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abstract embedding
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title embedding
sequence
Interhemispheric interaction in semantic categorization of pictures.
ies of the same picture) or semantically related pictures (e.g.; apple-banana). The stimuli were presented either unilaterally to the same hemisphere or bilaterally to the opposite hemispheres. The results from the two experiments showed a bilateral advantage in categorization of the semantically related pictures but not in categorization of the less demanding identical pictures. The results support the hypothesis that the cognitive capacity of the brain can be increased by dividing the processing of relati
10666556
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Interhemispheric interaction in semantic categorization of pictures.
vely demanding stimuli between the hemispheres.
10666556
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Primary task demands modulate P3a amplitude.
Auditory event-related brain potentials (ERPs) were recorded from 10 subjects in two different conditions: (1) subjects were required to reorder five visually presented letters in order to form a word and provide a verbal response (task condition); (2) subjects were presented with a control stimulus with the same physical characteristics as the experimental stimulus; but containing just one type of letter (i.e.; AAAAA). Subjects had to verbally respond to such stimuli by saying "A" (control condition). Tone
10666557
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Primary task demands modulate P3a amplitude.
s of 1000 Hz (standard) and 1050 Hz (deviant) were also presented to the subjects in a 85%-15% probability paradigm 2 s before; during and 8 s after the presentation of the visual stimuli. Recordings were obtained from Fpz; Fz; Cz and Pz vs. linked ears. Auditory ERPs to the auditory stimuli after the presentation of the visual letter string and during the performance of the task were averaged for the standard and deviant tones in both conditions. Only correct responses were considered for the averages. The
10666557
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0.009753617, -0.014908723, 0.026239352, -0.010893307, 0.01284138, -0.00033565334, 0.011887222, -0.06355754, 0.08110345, 0.049907777 ]
Primary task demands modulate P3a amplitude.
N100 was affected by stimulus type (standard vs. deviant) but not by condition (task vs. control); however; larger P3a waves were observed during the control than during the task condition. No significant differences between conditions were observed in the mismatch negativity (MMN) latency range. These results suggest that primary task demands modulate involuntary attention processing.
10666557
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Dopamine-antagonistic, anticholinergic, and GABAergic effects on declarative and procedural memory functions.
Declarative and procedural memory functions are related to dissociable neuroanatomic substrates. In the present study differential effects of pharmacologically induced changes in dopaminergic; GABAergic; and cholinergic activity in the brain on declarative (object and face recognition; immediate and delayed word recall) and procedural memory processes (compensatory tracking) were investigated. In a double-blind design; either 3 mg of haloperidol; 11 mg of midazolam; 1 mg of scopolamine; or placebo were admi
10666558
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Dopamine-antagonistic, anticholinergic, and GABAergic effects on declarative and procedural memory functions.
nistered to 80 healthy volunteers randomly assigned to one of the four drug conditions. Although all three drugs produced a detrimental effect on immediate and delayed word recall; recall performance was substantially more impaired by the benzodiazepine midazolam than by either haloperidol or scopolamine. While recognition of faces was affected by neither of the drugs; performance on object recognition was significantly decreased by midazolam as compared to placebo. Procedural learning was markedly impaired
10666558
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Dopamine-antagonistic, anticholinergic, and GABAergic effects on declarative and procedural memory functions.
by all drugs but; again; the observed effect was most pronounced with midazolam. Additional analyses of measures of subjective activation; cortical arousal; and psychomotor performance argued against the assumption that the observed memory-impairing effects were secondary to drug-induced sedation. The overall pattern of results revealed that memory processes are much more susceptible to changes in GABAergic than in dopaminergic or cholinergic neurotransmitter activity. Furthermore; the present findings poi
10666558
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Dopamine-antagonistic, anticholinergic, and GABAergic effects on declarative and procedural memory functions.
nt to the conclusion that the modulating effects of dopaminergic; GABAergic; and cholinergic neurotransmitter systems on declarative and procedural memory functions are less specific than suggested by neuropsychological studies in patients.
10666558
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-0.011256746, -0.016908199, 0.021352867, -0.00032539546, 0.055129696, -0.01432317, -0.036190405, -0.07074538, 0.008084809, -0.02301467, -0.06620839, 0.07027058, 0.019308584 ]
Functional asymmetry of human prefrontal cortex in verbal and non-verbal episodic memory as revealed by fMRI.
Functional neuroimaging studies have demonstrated preferential involvement of bilateral prefrontal cortex during episodic memory encoding and retrieval. The aim of the present study is to address the question whether left prefrontal model for encoding holds when highly non-verbal material is used; and which region of the brain is critically related to successful retrieval. To do this; seven normal subjects were investigated using functional magnetic resonance imaging (fMRI) during encoding and retrieval of
10666559
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Functional asymmetry of human prefrontal cortex in verbal and non-verbal episodic memory as revealed by fMRI.
word and checkerboard pattern. Our results revealed that word encoding activated the left prefrontal cortices and right cerebellum; whereas pattern encoding activated the bilateral middle frontal gyrus; superior parietal lobule; premotor area; and occipital visual cortex. Word-specific activation was found in the ventral prefrontal cortices; and pattern-specific activation located in the right dorsal prefrontal cortex. Conjunction analysis during encoding of word and pattern showed that activity in the left
10666559
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Functional asymmetry of human prefrontal cortex in verbal and non-verbal episodic memory as revealed by fMRI.
dorsal prefrontal cortex and the right cerebellum might relate to common neural network for encoding regardless of the type of material. Finally; the present study demonstrates strong association between the left ventral prefrontal cortex and retrieval success for word. The evidence; that both encoding and retrieval of words activated the left ventral prefrontal cortex; indicates that this area is involved in active and strategic operation of the mnemonic representation. A lack of the right prefrontal acti
10666559
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Functional asymmetry of human prefrontal cortex in verbal and non-verbal episodic memory as revealed by fMRI.
vation during retrieval was interpreted as that activity in this region might relate to retrieval effort rather than success.
10666559
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Hemispheric asymmetry for selective attention.
A letter-identification task; previously demonstrated to show activation of the pulvinar nucleus of the thalamus with fluodeoxyglucose position emission tomography; was administered to 20 normal volunteers. The letter to be detected could appear alone as a big stimulus or as a small one stimulus surrounded by flanking letters. To test for a hemispheric specialization for filtering processes; the stimuli were displayed horizontally; either in the left or in the right hemifield; or vertically; either above or
10666560
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0.04865328, -0.016271371, -0.008437255, 0.012190126, -0.02049335, -0.039271105, 0.01833545, 0.039190684, -0.050663743, 0.03208704, 0.028789874 ]
Hemispheric asymmetry for selective attention.
below the fixation point. In addition; to study the effect of cognitive processes on selective attention resources; we varied the feedback conditions; by delivering or not delivering a blue flash in cases of misses or mistakes. The results show a significant interaction between the type of stimulus (alone or surrounded by flankers) and the hemifield of presentation (left or right) only in the condition where the subjects were presented stimuli horizontally without any feedback. In this condition; reaction
10666560
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Hemispheric asymmetry for selective attention.
times (RTs) were shorter in the left hemifield than in the right hemifield for single stimuli; whereas for stimuli surrounded by flankers; the opposite pattern was observed; that is; shorter RT in the right hemifield than in the left one. The present findings suggest a hemispheric specialization for selective attention; in particular at the subcortical level.
10666560
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Mental rotation for spatial environment recognition.
We investigated the importance of retinal and body inclination in the recognition of spatial environment. The paradigm involved the recognition; in body upright and tilted conditions; of tilted images -intervals of 15 degrees from 0 degrees to 90 degrees leftward and rightward respective to head coordinates - of known spatial layouts encountered while walking in Paris. The analysis of reaction times was consistent with the subjects mentally rotating the spatial layout so that the environment was subjectivel
10666561
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Mental rotation for spatial environment recognition.
y vertical before making their decisions. In contrast; when the body was roll-tilted (33 degrees ); overall reaction time was not affected; however; reaction time and spatial layout tilt with respect to the head were correlated when the body was tilted but not when upright. Both results indicate that gravity was slightly important in performing the task.
10666561
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Prefrontal cortex activation in task switching: an event-related fMRI study.
When a switch between two tasks has to be carried out; performance is slower than in trials where the same task is performed repeatedly. This finding has been attributed to time-consuming control processes required for task switching. Previous results of other paradigms investigating cognitive control processes suggested that prefrontal cortex is involved in executive control. We used event-related fMRI to investigate prefrontal cortex involvement in task switching. Regions in the lateral prefrontal and pre
10666562
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0.042301703, 0.023533484, 0.057396144, 0.0097767785, -0.018209167, -0.03553982, 0.026914425, 0.019473692, 0.07837395, 0.03450158, -0.044883996, -0.036817655, -0.011054615, 0.038468197, -0.067405865, 0.0032062375, -0.036178738, -0.012252586, -0.01298468, 0.017543627, -0.058301277, 0.0589402, 0.04829156, -0.28282776, -0.017130991, -0.00022253983, 0.027846182, -0.03974603, -0.010542149, 0.06351911, 0.013470524, -0.03386266, -0.01174012, -0.087265566, 0.019806461, 0.060111545, 0.034474958, 0.0069415793, 0.01707775, 0.07661693, -0.083804764, 0.006272712, 0.017583558, 0.01926072, 0.01375005, 0.17964248, 0.004246143, -0.0499421, 0.08172828, 0.032425094, -0.00007825291, -0.0850826, -0.01174012, 0.011453939, 0.033942524, 0.025623279, -0.047679264, -0.0041363295, 0.04243481, 0.02546355, -0.02328058, 0.013530422, -0.0035473267, 0.014442212, -0.03716374, -0.102865815, 0.0072144503, 0.10850959, -0.08061017, -0.029629828, 0.0055805505, 0.012871538, 0.0071146195, -0.029310368, -0.029523341, -0.0054907026, 0.010615358, 0.020192474, 0.0033210432, -0.034980766, 0.013949713, -0.0009858307, 0.002628882, -0.029230503, 0.03101415, 0.0042361603, 0.07171856, 0.10606041 ]
Prefrontal cortex activation in task switching: an event-related fMRI study.
motor cortex bilaterally; the anterior insula bilaterally; the left intraparietal sulcus; the SMA/pre-SMA region and the cuneus/precuneus were activated by the task repetition condition and showed additional activation in the task switch condition. This confirmed the hypothesis that lateral prefrontal cortex is involved in task switching. However; the results also showed that this region is neither the only region involved in task switching nor a region specifically involved in task switching.
10666562
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0.040068746, 0.037031233, -0.035182312, 0.0033742797, 0.01835714, 0.033439048, 0.018066594, 0.03573699, 0.035287965, -0.007871118 ]
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-0.014803418, 0.082455434, -0.09154085, 0.048860524, 0.003902239, -0.0046747634, -0.037979152, 0.009943777, 0.027256249, -0.00919106, -0.019544208, -0.04106925, -0.009679666, 0.00059796363, -0.011970828, -0.023968067, 0.0072828587, -0.01026071, -0.008253466, -0.018184038, 0.01995358, 0.051290344, 0.014750595, 0.120857164, 0.00371406, -0.036368076, -0.016889894, 0.014301607, 0.039246883, -0.06930271, -0.09164649, -0.040963605, -0.01057104, 0.030584047, -0.044291403, 0.0022465936, -0.011673703, -0.03116509, 0.019557415, 0.017801076, -0.07099302, -0.014948679, 0.0068272674, -0.00039596006, 0.057523362, 0.028101403, 0.055040717, 0.018078392, -0.007164009, -0.018923549, -0.036130376, -0.049573623, -0.028365513, 0.0017216732, 0.027150603, -0.0061900998, -0.041967228, -0.0129810525, 0.0028821107, -0.014077113, 0.0319046, -0.05414274, -0.058791094, 0.07088737, -0.028127814, 0.052769363, 0.0128556, 0.034651354, 0.04421217, -0.041280538, 0.03676424, 0.06718982, 0.019768704, -0.02440385, -0.01026071, -0.012155706, 0.013132916, -0.024113327, 0.060006004, -0.027335482, -0.027467538, 0.026186598, -0.0011670402, 0.019134836, 0.004747394, -0.0614322, -0.0003501533, 0.048622824, -0.0071111866, -0.032961044, 0.029633246, 0.011805759, -0.002707137, -0.28228176, 0.013786591, 0.048305888, 0.020151664, 0.0005892975, 0.016480522, 0.02425859, 0.016533345, -0.047143802, 0.01630885, 0.01835571, 0.043340605, 0.059583426, 0.014948679, -0.015384462, -0.005103944, 0.031217912, -0.060481403, -0.03409672, -0.03549651, 0.018699054, -0.0452422, 0.17705996, -0.02668841, 0.019438565, 0.053984273, -0.0027731648, -0.0055463295, -0.0016440905, 0.010293723, -0.08277237, 0.06602773, 0.02259469, -0.0036315252, 0.051316753, 0.0103927655, -0.00042422817, -0.028682448, -0.05609716, 0.044185758, -0.030399168, -0.006840473, -0.08176874, -0.023624722, 0.04949439, -0.08504372, -0.0633338, -0.05609716, 0.018368915, -0.030742513, -0.040118452, -0.07775426, 0.040250506, -0.010709698, -0.023202145, 0.039986394, 0.037028354, -0.035205986, 0.003369065, 0.018329298, 0.03341003, 0.018091599, 0.035707798, 0.03531163, -0.007916725 ]
Early and late components of visual categorization: an event-related potential study.
We examined the characteristics of early and late components of event-related potentials (ERPs) accompanying the visual categorization of natural scenes. In the first experiment; ERPs were recorded in an animal-non-animal categorization task (CT); whereas the second experiment included a spatial frequency discrimination task (DT). In the CT; there were more negative potentials for non-animals in the time windows of 150-250 ms (N1) and 350-500 ms (N2); and a more positive potential for animals in the time wi
10666564
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Early and late components of visual categorization: an event-related potential study.
ndow of 250-350 ms (P2). In the DT; spatial frequency gratings evoked only a short-duration difference N1 at the frontal sites. Our results suggest that N1 may be related to higher-level categorization processes.
10666564
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Different cortical activity in reading of Kanji words, Kana words and Kana nonwords.
We report a positron emission tomography study on reading of Japanese Kanji (morphograms) words; Kana (phonograms) words and Kana nonwords using statistical parametric mapping. Activity was more pronounced in the lateral fusiform gyrus (Area 37) in Kanji; in contrast to the greater activation in the middle and inferior occipital gyri (Areas 18 and 19) and the deep perisylvian temporo-parietal area (Areas 40/22 and 22/21) in Kana; suggesting that Kanji and Kana are processed differently.
10666563
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Activity of the phosphatidylcholine biosynthetic pathway modulates the distribution of fatty acids into glycerolipids in proliferating cells.
PtdCho accumulation is a periodic; S phase-specific event that is modulated in part by cell cycle-dependent fluctuations in CTP:phosphocholine cytidylyltransferase (CCT) activity. A supply of fatty acids is essential to generate the diacylglycerol (DG) precursors for phosphatidylcholine (PtdCho) biosynthesis but it is not known whether the DG supply is also coupled to the cell cycle. Although the rate of fatty acid synthesis in a macrophage cell line was dramatically stimulated in response to the growth fac
10666565
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0.026389085, -0.01931776, 0.009395516, 0.013240632, 0.010534565, -0.0062153935, -0.04008402, -0.01570967, 0.061627205, 0.032077752 ]
Activity of the phosphatidylcholine biosynthetic pathway modulates the distribution of fatty acids into glycerolipids in proliferating cells.
tor; CSF-1; it was not regulated by the cell cycle. Increased fatty acid synthesis correlated with elevated acetyl-CoA carboxylase (ACC) and fatty acid synthase (FAS) steady-state mRNA levels. Cellular fatty acid synthesis was essential for membrane PL synthesis. Cerulenin inhibition of endogenous fatty acid synthesis also inhibited PtdCho synthesis; which was not relieved by exogenous fatty acids. Inhibition of CCT activity by the addition of lysophosphatidylcholine (lysoPtdCho) or temperature-shift of a c
10666565
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0.023312528, -0.028674012, -0.023590531, -0.003551156, -0.02899173, -0.013132327, 0.04204463, -0.017130272, 0.07386934, 0.0013982883 ]
[ -0.041224748, -0.031031087, -0.017236551, -0.023908764, 0.0030365852, -0.049644444, 0.018785458, 0.025034038, -0.06497465, 0.020559419, 0.029389512, -0.09102805, -0.04228383, 0.053854294, -0.04890309, -0.022055373, -0.03126938, 0.032116644, -0.000055384582, 0.013152468, 0.07461229, -0.01564793, -0.025907781, -0.05967924, 0.06804599, 0.06508055, 0.004130418, 0.009372871, -0.025947496, -0.18353882, -0.005613132, 0.0049545155, -0.009544971, -0.0766775, -0.033652313, -0.04630834, 0.008432936, -0.017474845, -0.033652313, 0.013437096, -0.032831527, 0.0009581378, -0.047023218, 0.02439859, -0.0056727054, -0.0063379407, 0.011371887, -0.0066258786, 0.025047276, -0.013926921, 0.0059076888, 0.046758447, 0.011709469, 0.0021479495, -0.021552308, -0.009856077, 0.038391702, 0.02867463, 0.025709203, -0.008068877, 0.006423991, 0.04397836, -0.16394581, 0.034473103, 0.046255384, 0.030475069, 0.034393672, -0.033599358, -0.04503744, -0.020135786, -0.02949542, 0.055389963, 0.024583928, 0.0022571674, 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Activity of the phosphatidylcholine biosynthetic pathway modulates the distribution of fatty acids into glycerolipids in proliferating cells.
onditionally defective CCT diverted newly synthesized DG to the TG pool where it accumulated. Enforced expression of CCT stimulated PtdCho biosynthesis and reduced TG synthesis. Thus; the cellular DG supply did not regulate PtdCho biosynthesis and CCT activity governs the partitioning of DG into either the PL or TG pools; thereby controlling both PtdCho and TG biosynthesis.
10666565
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The major low molecular weight apolipoprotein from normal and hyperlipidemia atherosclerosis-prone (LAP) Japanese quail.
The low molecular weight (LMW) apolipoprotein of apo C plays an important role in the metabolism of triglyceride-rich lipoproteins. This study aimed at a characterization of the major LMW apolipoproteins from normal quail strain; and also from LAP (hyperlipidemia atherosclerosis-prone) strain to identify its genetic disorder. The major LMW apoprotein cDNA clone from normal quail comprised of approximately 500 bp; and encoded polypeptide of 78 amino acid residues containing 57 amino acids as a mature apolipo
10666566
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The major low molecular weight apolipoprotein from normal and hyperlipidemia atherosclerosis-prone (LAP) Japanese quail.
protein. Although the quail LMW apoprotein showed a low homology to either apo C-I; C-II; or C-III of other animals; it retained a well-developed amphipathic alpha-helix structure. There was no difference in the deduced primary structure of the quail LMW apoprotein between LAP and normal strain. An analysis of the mRNA expression showed that the quail LMW apoprotein was only expressed in the liver of both LAP and normal Japanese quail. No difference was noted in the hepatic expression of the quail LMW apopr
10666566
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0.0066152257, 0.01974635, -0.009078553, -0.0010139705, 0.0034930247, -0.030486986, 0.0047677304, -0.027149575 ]
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The major low molecular weight apolipoprotein from normal and hyperlipidemia atherosclerosis-prone (LAP) Japanese quail.
otein mRNA between normal and LAP strains with neither normal nor atherogenic dietary conditions. The structure and expression of the major LMW apoprotein thus had no relevance to higher susceptibility of LAP strain to the experimental atherosclerosis.
10666566
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-0.025244309, -0.005119243, -0.09757769, 0.00062787085, 0.050833885, -0.048762284, -0.0053184354, -0.046504773, 0.04262716, -0.0066131856, -0.031897333, 0.09439061, 0.05152442 ]
Purification and regiospecificity of multiple enzyme activities of phospholipase A(1) from bonito muscle.
Phospholipase A(1) (PLA(1)); which catalyzes the hydrolysis of the sn-1 ester bond of diacyl phospholipids; was purified from 100;000 x g supernatant of bonito muscle to homogeneity by ammonium-sulfate precipitation and four consecutive column chromatographies (DEAE anion-exchange; ether-Toyopeal; hydroxylapatite and Toyopeal HW 50S columns). The final preparation showed a single band above the 67-kDa molecular marker on SDS-PAGE; and the molecular mass was determined to be 71.5 kDa by matrix-assisted laser
10666567
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0.015982226, 0.062091555, -0.0185356, 0.04261026, 0.04623092, -0.00920025, 0.033315443, -0.013712561, -0.06122692, -0.026709095, 0.013138389 ]
Purification and regiospecificity of multiple enzyme activities of phospholipase A(1) from bonito muscle.
desorption/ionization time-of-flight mass spectrometry using bovine serum albumin as a standard for calibration. The N-terminal 8 amino residues were determined to be Ala-Pro-Ala-Glu-Lys-Val-Lys-Try. Regiospecificity of multiple enzyme activities of the PLA(1) was examined using positionally defined synthetic phosphatidylcholine (PC) and lysophosphatidylcholines (LPC). An acyl ester bond at the sn-1 position of PC was exclusively hydrolyzed by phospholipase activity; and 1-acyl LPC was cleaved to fatty aci
10666567
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Purification and regiospecificity of multiple enzyme activities of phospholipase A(1) from bonito muscle.
d and glycerophosphocholine by lysophospholipase (LPL) activity. However; the positional isomer; 2-acyl LPC was a poor substrate for LPL activity. PC/transacylation activity was also observed when excess 2-acyl LPC was supplied in the reaction mixture; and fatty acid at the sn-1 position of donor PC was transferred to the sn-1 position of acceptor LPC. These results demonstrate that the multiple enzyme activities of PLA(1); this is lysophospholipase; transacylase as well as phospholipase; have a strict regi
10666567
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Purification and regiospecificity of multiple enzyme activities of phospholipase A(1) from bonito muscle.
ospecificity at the sn-1 position of substrates.
10666567
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Phosphocholine and phosphoethanolamine during chick embryo myogenesis: a (31)P-NMR study.
Elevated contents of phosphoethanolamine (Etn-P) and/or phosphocholine (Cho-P); a common feature of most tumours with respect to normal counterparts; may also occur in non-cancerous proliferating tissues. The significance of these alterations in relation to cell proliferation; differentiation and maturation is scarcely understood. In this work; the Cho-P and Etn-P pools were measured by (31)P-NMR in extracts of chick embryo pectoral muscle at different days of development. The average concentration of these
10666568
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-0.011644087, -0.006486947, 0.017836623, 0.014515412, -0.057267733, 0.014250774, 0.04231567, -0.022084069, -0.009976865, 0.060390465, 0.024055624 ]
Phosphocholine and phosphoethanolamine during chick embryo myogenesis: a (31)P-NMR study.
metabolites exhibited the highest values (respectively; 1.5 and 3.0 micromol/mg DNA) on days 9-11 and decreased at later stages of myogenesis. While; however; Cho-P maintained substantial levels (above 1.0 micromol/mg DNA) also during myotube formation (days 11-18) and stepwise decreased (to about 0.5 micromol/mg DNA) upon fibres' maturation; Etn-P gradually decreased between day 11 and hatching time (down to about 0.2 micromol/mg DNA). These results demonstrate that significant changes may occur in the st
10666568
[ -0.10234377, -0.021323819, -0.033727523, -0.01739158, -0.03240798, -0.0069078086, 0.041116968, -0.006732969, -0.012106809, 0.013307593, 0.005456311, -0.034123387, 0.037686154, 0.014554561, 0.052042782, 0.014145503, -0.013439547, 0.0010770771, -0.050855197, -0.008979492, 0.049746778, 0.038926523, -0.065238215, 0.018843077, 0.056634795, 0.05953779, 0.016995717, -0.05589585, -0.055104125, -0.213766, 0.015227528, -0.03240798, 0.036287438, -0.0635492, -0.039269608, 0.038847353, 0.014119112, 0.024160836, -0.03304136, 0.037818108, 0.07875034, 0.002741351, -0.008880526, -0.012251958, 0.035152633, -0.00016855102, -0.07838087, 0.034387294, 0.031484302, -0.015069184, -0.034624815, -0.007620362, 0.007013372, -0.010463977, -0.002652282, 0.0045986082, 0.02778958, 0.06344364, 0.02105991, 0.022221107, 0.09806845, 0.01045738, -0.117281, 0.075002834, 0.04668544, 0.060540643, 0.035205413, -0.06291582, -0.009744827, 0.074158326, 0.030032804, 0.023144787, 0.018130524, 0.0413017, -0.022049567, 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-0.012523475, 0.0192141, 0.0077859326, -0.009052796, 0.004684756, -0.050832905, -0.021523485, -0.032621738, 0.0059417225, -0.014898844, 0.09221712, 0.0031671592 ]
Phosphocholine and phosphoethanolamine during chick embryo myogenesis: a (31)P-NMR study.
eady-state pools of these metabolites during normal in vivo cellular development and differentiation; and are consistent with: (a) high rates of phospholipid biosynthesis reported in the literature for proliferating myoblasts; (b) sustained phosphatidylcholine synthesis maintained also during myoblast fusion; and (c) decreased requirement of phospholipid synthesis in the last phase of in ovo myofibre maturation.
10666568
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The contribution of newly synthesized cholesterol to bile salt synthesis in rats quantified by mass isotopomer distribution analysis.
A new stable isotope procedure has been developed and validated in rats; applying [1-(13)C]acetate infusion to quantify the production of bile salts from de novo synthesized cholesterol making use of the mass isotopomer distribution analysis (MIDA) principle. Ions (m/z) 458-461; 370-373 and 285-288 were monitored by GC/MS (EI-mode) for the methyl trimethylsilylether derivatives of cholate; chenodeoxycholate and beta-muricholate; respectively. Rats with intact exteriorized enterohepatic circulation and rats
10666569
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The contribution of newly synthesized cholesterol to bile salt synthesis in rats quantified by mass isotopomer distribution analysis.
with chronic bile diversion were infused with [1-(13)C]acetate for up to 14 h. After 10 h of infusion the enterohepatic circulation of the intact group was interrupted to deplete the existing bile salt pool (acute bile diversion). The fractions of biliary cholesterol and individual bile salts derived from newly synthesized cholesterol were determined by MIDA at t=14 h. In rats with acute bile diversion; these fractions were 20; 25; 27 and 23% for biliary cholesterol; cholate; chenodeoxycholate and beta-muri
10666569
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The contribution of newly synthesized cholesterol to bile salt synthesis in rats quantified by mass isotopomer distribution analysis.
cholate; respectively. After bile diversion for 8 days to induce hepatic cholesterol and bile salt synthesis; these fractions increased significantly to 32; 47; 41 and 47%; respectively. Calculated enrichments of the acetyl-CoA precursor pools were similar for all bile salts and biliary cholesterol within the two rat groups. However; chronic enterohepatic interruption decreased the acetyl-CoA pool size almost two-fold. We conclude that MIDA is a validated new stable isotope technique for studying the synthe
10666569
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-0.011778369, -0.0042461627, -0.033347253, -0.007383455, -0.015564756, 0.021082062, 0.01818818, 0.064855404, -0.051251452, 0.081082776, 0.0111698415 ]
The contribution of newly synthesized cholesterol to bile salt synthesis in rats quantified by mass isotopomer distribution analysis.
tic pathway from acetyl-CoA to bile salts. This technique provides an important new tool for studying bile salt metabolism in humans using stable isotopes.
10666569
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Intestinal fatty acid binding protein may favor differential apical fatty acid binding in the intestine.
The intestinal mucosa metabolizes fatty acids differently when presented to the lumenal or basolateral membrane. Expression of both liver and intestinal fatty acid binding proteins (L- and I-FABPs) uniquely in the enterocyte offers a possible explanation of this phenomenon. An organ explant system was used to analyze the relative binding of fatty acids to each protein. More fatty acid was bound to L-FABP than to I-FABPs (28% vs. 6% of cytosolic radioactivity); no matter on which side the fatty acid was adde
10666570
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Intestinal fatty acid binding protein may favor differential apical fatty acid binding in the intestine.
d. However; a 2-3-fold increase in fatty acid binding to the intestinal paralog was noted after apical addition of palmitic or oleic acid in mucosa from chow fed rats. When oleic acid was added apically; a 1.4-fold increase in binding to I-FABP was observed in mucosa derived from chronically fat fed rats; consistent with the previously observed 50% increase in the content of that protein. Immunocytochemical localization of both FABPs in vivo demonstrated an apical cytoplasmic localization in the fasting sta
10666570
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Intestinal fatty acid binding protein may favor differential apical fatty acid binding in the intestine.
te; and redistribution to the entire cytoplasm after fat feeding. These data are consistent with the hypothesis that I-FABP may contribute to the metabolic compartmentalization of apically presented fatty acids in the intestine.
10666570
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Use of differentially substituted selenomethionine proteins in X-ray structure determination.
Using heavily methionine-substituted T4 lysozyme as an example; it is shown how the addition or deletion of a small number of methionines can simplify the location of selenium sites for use in MAD phasing. By comparing the X-ray data for a large number of singly substituted lysozymes; it is shown that the optimal amino acid to be substituted by methionine is leucine; followed; in order of preference; by phenylalanine; isoleucine and valine. The identification of leucine as the first choice agrees with the r
10666571
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-0.017574113, -0.06539939, -0.011814806, -0.04594281, -0.013348427, 0.010695855, 0.034674317, -0.040835127, 0.009142487, 0.031409614 ]
Use of differentially substituted selenomethionine proteins in X-ray structure determination.
anking suggested by the Dayhoff mutation probability; i.e. by the frequency of amino-acid substitutions in the sequences of related proteins. The ranking of the second and subsequent choices; however; differ significantly.
10666571
[ -0.07447716, -0.047991686, -0.058532905, 0.006634612, -0.028763227, 0.005604989, 0.06377703, 0.04385995, -0.007839701, -0.020724885, 0.024472581, -0.05874479, 0.045740418, -0.020155448, 0.011633745, -0.011209978, -0.048812736, 0.02693573, -0.07966831, 0.03514623, 0.08613077, -0.039092563, 0.0073497198, -0.038430426, 0.027995149, 0.0461377, 0.0058301156, 0.03752992, -0.021122169, -0.2100828, -0.011084172, -0.052070446, -0.020393817, -0.036046736, -0.021453237, -0.010236637, 0.04907759, -0.033398185, -0.04473397, 0.008137663, 0.0769668, -0.0032461262, 0.022949666, -0.004346929, 0.0131169325, 0.06330029, -0.056996748, -0.0043072007, 0.08242281, -0.021598907, 0.010627298, -0.0032262623, -0.009501665, 0.052917983, -0.014249187, -0.00036376147, 0.007866187, 0.0048766383, -0.025015533, 0.010792832, 0.013759205, 0.0070517585, -0.10530626, 0.08454164, 0.034351666, -0.009475179, -0.036761843, 0.049766213, 0.025876312, 0.030961523, -0.044760454, -0.013613535, -0.034457605, -0.017996881, 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[ -0.07447721, -0.047991715, -0.058532942, 0.00660482, -0.028763246, 0.0056049926, 0.06377707, 0.043859977, -0.0078463275, -0.020764627, 0.024552053, -0.058797795, 0.04560802, -0.020181946, 0.01162051, -0.011209985, -0.048812766, 0.026962232, -0.079668365, 0.035119765, 0.086077854, -0.039119072, 0.007309996, -0.038483422, 0.027995167, 0.046084758, 0.0058897114, 0.03750346, -0.021135423, -0.21008293, -0.011110664, -0.052096967, -0.02039383, -0.03607324, -0.021440007, -0.010256507, 0.049051132, -0.033451177, -0.044681028, 0.008111183, 0.07701982, -0.0032246087, 0.022989409, -0.004310514, 0.013044106, 0.06340627, -0.05704975, -0.004350242, 0.082581766, -0.02159892, 0.010647168, -0.003216332, -0.009481806, 0.052865043, -0.014262438, -0.0004018346, 0.007886056, 0.004879952, -0.02506852, 0.010819324, 0.013772457, 0.0070650056, -0.10535929, 0.08454169, 0.034351684, -0.009442078, -0.03673538, 0.049819212, 0.025836598, 0.030988026, -0.044733997, -0.013573815, -0.034457628, -0.01798365, 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-0.0068465, -0.010051245, -0.06059881, 0.056573015, 0.0719346, -0.0037013476, 0.026975475, 0.07537772, 0.08756104 ]
Three-dimensional structure of the Gly121Tyr dimeric form of ornithine decarboxylase from Lactobacillus 30a.
Ornithine decarboxylases catalyze the conversion of ornithine to putrescine at the beginning of the polyamine pathway. Ornithine decarboxylase (ODC) from Lactobacillus 30a is a 990612 Da dodecamer composed of six homodimers. A single point mutation (Gly121Tyr) was found to prevent association of dimers into dodecamers. The dimeric protein has been crystallized at pH 7.0 in the presence of guanosine triphosphate (GTP). Crystals belong to space group P3(2)21; with unit-cell parameters a = 111.8; c = 135.9 A a
10666573
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0.013952094, -0.0078115813, -0.0016694105, -0.009217401, -0.0033537413, -0.014403018, -0.045861542, -0.009781055, -0.010901731, -0.002947579, 0.07082147, -0.0016213342 ]
Three-dimensional structure of the Gly121Tyr dimeric form of ornithine decarboxylase from Lactobacillus 30a.
nd one monomer in the asymmetric unit. The structure was determined by molecular replacement and refined using simulated annealing to R = 0.211 at 2. 7 A resolution. The GTP-binding site was analyzed in detail. The protein exhibits a novel binding mode for GTP which is different from that seen in most G-proteins or GTPases. Central to this binding scheme appear to be three lysines; Lys190; Lys374 and Lys382; which form salt bridges with the three phosphates; and Thr191; which hydrogen bonds with the guanine
10666573
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Three-dimensional structure of the Gly121Tyr dimeric form of ornithine decarboxylase from Lactobacillus 30a.
base. Furthermore; the structure suggests that there is some flexibility in the wing domain; which can change its orientation as the protein adapts to its environment. The active site is similar to that of the native enzyme; consistent with the observation that the enzyme activity does not depend on its dodecameric state.
10666573
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Structure of taq DNA polymerase shows a new orientation for the structure-specific nuclease domain.
Thermus aquaticus DNA polymerase I consists of the polymerase; the structure-specific nuclease and the vestigial editing nuclease domains. Three-dimensional structures of the native enzyme and its complex with DNA have already been reported. The structure of a complex with an inhibitory antibody has also been determined. The structure of the native enzyme in a different crystal form determined at 2.6 A is reported here. Optimized anomalous diffraction measurements made at the holmium L(III) edge were valuab
10666572
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-0.007487951, 0.008719303, -0.017451918, 0.07731559, 0.0024044642, -0.018490247, 0.0066526285, -0.008978886, 0.00610684, 0.008193483, 0.020620152, 0.009045444, 0.017505165, -0.039962362, 0.03186872, -0.017585037, -0.015681433, 0.021764977, 0.01005715, 0.023415655, -0.0026357588, -0.015002525, -0.28945422, 0.027449165, -0.0103966035, 0.020380538, -0.034424607, -0.052795045, 0.05713473, 0.008200138, -0.07571816, -0.013724582, -0.023269223, 0.0029302847, 0.012925867, -0.04440854, 0.0048189126, 0.0040102135, 0.13972184, -0.04691118, 0.0064662616, -0.075877905, 0.009983934, 0.010290109, 0.23705855, -0.030324537, 0.008739271, 0.052582055, 0.053647008, 0.047603402, -0.059051644, 0.053833377, -0.0016964369, -0.00031719793, 0.01942208, -0.047709897, 0.05087813, 0.02909984, -0.014896031, -0.0158678, 0.024973148, -0.0021215861, -0.054099616, -0.0017105808, -0.08855084, 0.013571495, 0.1245995, -0.0005033567, 0.0000030159802, 0.006579413, 0.028567364, -0.0062199915, 0.007674318, 0.08535598, 0.003936998, 0.03889741, -0.049307324, -0.03871104, -0.06895571, 0.038364932, 0.03937664, 0.00396695, -0.019075971, -0.0015441818, -0.0322947, -0.02163186, -0.038151942 ]
Structure of taq DNA polymerase shows a new orientation for the structure-specific nuclease domain.
le in validating solutions obtained through molecular replacement. The structure of the polymerase domain is similar to those reported previously; while the relative orientation of the structure-specific nuclease domain is significantly different from those of the native enzyme and the DNA complex; it is; however; identical to that observed in the structure of the Fab complex. In the structures of the native enzyme and of the DNA complex reported previously; the active site of the structure-specific nucleas
10666572
[ 0.030526511, 0.027201584, 0.047700945, -0.008004701, -0.022868704, 0.04400949, 0.00008375728, 0.017959852, 0.034060884, 0.037778523, 0.0096278945, -0.020172108, -0.006728399, 0.025866374, -0.006813486, 0.046182476, -0.015813047, -0.013666242, -0.04256956, 0.037438173, 0.018627455, 0.0034361961, -0.021009885, -0.032804217, 0.009575533, 0.06440413, -0.032542415, -0.023902835, -0.013914958, -0.028772416, 0.02226655, -0.030683596, 0.020918252, 0.003868175, -0.008829388, -0.013024819, -0.014333847, 0.020682627, -0.10404147, -0.032175887, 0.064823024, -0.03717637, -0.016847178, -0.081212044, -0.017030442, -0.012376851, 0.0056844503, -0.017828949, 0.03180936, -0.049690668, -0.028170263, -0.016271207, 0.0047583133, -0.0021697124, -0.021978565, 0.058539692, 0.0734626, -0.039296992, -0.0023006152, 0.025565298, 0.048015114, 0.016362838, -0.1662988, 0.0762901, 0.04942886, 0.05613108, -0.004208522, 0.008187965, 0.037987966, 0.010799473, 0.045292336, -0.04783185, 0.047570046, 0.06587024, 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-0.0012550297, 0.0030336704, 0.03379908, 0.012331035, 0.00046265926, -0.07969357, 0.0011740336, -0.0004491599, 0.005331013, 0.019988844, 0.026259083, 0.06372344, 0.03180936, -0.02895568, -0.01354843, 0.09351689, 0.013090271, -0.055712193, -0.0064993193, -0.025565298, 0.09514009, -0.015917769, -0.019386692, 0.0067807604, 0.053931914, -0.035972062, 0.048617266, 0.032202065, -0.010668571, -0.0017360972, 0.023353044, -0.011833604, 0.068226494, -0.03615533, -0.05275379, 0.057649553, 0.00088441145, -0.012187042, -0.0678076, 0.011172546, -0.003130211, 0.04927178, -0.035422273, 0.104408, -0.04160088, -0.008534856, -0.03961116, -0.031181024, 0.014792006, -0.006950934, -0.057806637, 0.050659347, -0.033982344, -0.0055928184, -0.015603603, 0.06927371, 0.045737408, -0.0005632907, -0.010799473, 0.018274019, 0.006692401, 0.05272761, -0.0329613, -0.024413355, 0.09315037, 0.019543774, -0.026717244, -0.053879555, -0.0012231222, 0.024583528, -0.018260928, -0.015210895, 0.020970615, 0.013901868, 0.047072615, -0.31102484, 0.050502267, 0.06613205, -0.07246774, 0.05843497, 0.024217, 0.036024425, -0.0023840657, -0.022659259, -0.02412537, -0.00094495394, -0.022305822, 0.010354404, -0.027987, -0.023339953, -0.043930948, 0.004784494, 0.046732266, 0.025944917, 0.012619021, -0.00918937, 0.005776082, 0.0011478531, -0.05081643, -0.005406282, -0.019674677, 0.1909085, 0.11980216, -0.014569472, -0.019268878, 0.06052941, 0.039296992, -0.09032287, -0.14734408, 0.038380675, 0.07377677, -0.023876654, 0.025460577, -0.00581208, -0.010380585, 0.03432269, 0.0021353504, 0.029610192, -0.060791217, 0.015223985, -0.03382526, -0.029793456, 0.004921942, -0.014360027, 0.034008525, 0.0070687463, -0.07079218, 0.0073043713, 0.042176854, 0.0030385791, -0.0041692513, -0.025277313, -0.054455526, 0.007945795, 0.022934154, -0.017383879, 0.019412871, -0.020381551, -0.052020736, -0.0047812215, 0.05264907, -0.027175402, -0.064980105, 0.012422667, -0.016310478, -0.06293802, -0.008665759, -0.00991588, -0.08147384, 0.032725677, 0.03783088, 0.010511488, -0.0016551011, -0.084772594, 0.028274985, 0.019687768, -0.0019013619, 0.015839228, -0.004732133, 0.005723721, 0.022921065, -0.037281092, -0.010164595, 0.014216034, -0.037124008, -0.04974303, 0.032647137, -0.046522822, -0.07094927, -0.021114606, -0.044794906, -0.35040036, 0.027568111, 0.011964507, 0.03335401, -0.046444282, 0.060215246, 0.004967758, 0.06607968, -0.064508855, 0.025866374, -0.04400949, -0.017632594, 0.032254428, 0.066917464, 0.010419856, 0.016074853, -0.0038321768, -0.07382913, 0.0053866464, 0.0115914345, 0.026232902, -0.0034852845, 0.13634826, -0.014386208, 0.002552603, 0.012573205, -0.032673314, 0.005164112, 0.030369429, -0.04154852, 0.041862685, -0.01590468, 0.03783088, 0.010419856, -0.020617176, 0.014831277, 0.008515221, 0.025264222, 0.03950644, 0.044664003, -0.07644718, -0.020577906, 0.01691263, -0.037281092, 0.053879555, 0.0378047, 0.013234264, -0.05518858, 0.01691263, -0.02271162, 0.0178944, 0.0032169342, 0.028301166, 0.031207206, 0.04631338, -0.00059397105, 0.00867885, 0.0132015385, -0.011519439, -0.025368946, -0.03804033, -0.06613205, 0.039061368, -0.012592841, 0.012769559 ]
[ 0.030500911, 0.027254462, 0.047754217, -0.00791322, -0.022803687, 0.044036508, 0.00011781468, 0.017960193, 0.034061532, 0.03777924, 0.00968044, -0.020198673, -0.0066990736, 0.025814505, -0.0068594324, 0.046235718, -0.01583953, -0.013731956, -0.042622734, 0.037412707, 0.0186409, 0.0034297162, -0.020957923, -0.032831024, 0.009628077, 0.064353, -0.032595396, -0.023942562, -0.013875951, -0.028799145, 0.022240793, -0.030736541, 0.020957923, 0.0039140657, -0.008764103, -0.013005432, -0.014294848, 0.02064375, -0.104043454, -0.032124136, 0.06482425, -0.03717708, -0.016834408, -0.08116122, -0.016978405, -0.012403267, 0.005678013, -0.01785547, 0.031862326, -0.049691614, -0.028144618, -0.016245335, 0.004692951, -0.0021108463, -0.022005165, 0.05859317, 0.073464, -0.03927156, -0.0024004742, 0.025578877, 0.047989845, 0.016336968, -0.16630197, 0.07623919, 0.049429804, 0.056079786, -0.00421842, 0.008181575, 0.038067233, 0.010865131, 0.045319382, -0.0477804, 0.04757095, 0.06592386, -0.025997773, -0.06822779, -0.017083129, -0.035056412, -0.034846965, -0.04628808, -0.011997461, 0.020237943, -0.011009127, 0.024361458, -0.0009801526, -0.041235138, -0.008476112, -0.021861168, 0.034585156, -0.017240215, -0.021376818, 0.0021959348, -0.07482541, 0.049560707, -0.020604478, 0.0047453134, 0.018313637, -0.035553854, -0.012128367, 0.3355362, -0.043224897, 0.018025646, 0.103834, -0.006456899, 0.005540563, -0.0023661116, 0.009359722, -0.03649637, -0.011526203, 0.050241414, -0.012606171, -0.029034773, -0.016965315, -0.03304047, -0.01006661, 0.039507188, 0.00718015, 0.038695578, -0.02642976, -0.07403998, 0.08304626, 0.030317644, -0.026089406, -0.031548154, 0.002317022, 0.027568635, 0.12755403, 0.10650447, 0.040109355, -0.006244178, 0.014923193, -0.023366578, -0.009811345, 0.03419244, -0.021298276, -0.058959704, 0.00050971215, 0.0134439645, 0.048173115, 0.054666013, -0.0254087, -0.056289237, -0.06309631, -0.10561431, -0.07398762, 0.09618914, -0.025225433, 0.0048794914, -0.0012542354, 0.0029617301, 0.03377354, 0.01234436, 0.0004868037, -0.079747446, 0.0011748741, -0.0005043941, 0.005272207, 0.019989224, 0.026311945, 0.063777015, 0.031836145, -0.02893005, -0.013548688, 0.09357104, 0.013044703, -0.055765614, -0.0064503537, -0.025591966, 0.0951419, -0.015957344, -0.01938706, 0.0067677987, 0.05388058, -0.03602511, 0.04861819, 0.0321765, -0.010622957, -0.0017230397, 0.023327306, -0.0118469205, 0.06822779, -0.036156017, -0.052754797, 0.05770301, 0.00090733665, -0.012167638, -0.0678089, 0.011218576, -0.0031597242, 0.049272716, -0.035370585, 0.104409985, -0.041680217, -0.0085612, -0.039664276, -0.031129256, 0.014792288, -0.0070034284, -0.057807736, 0.050712675, -0.03395681, -0.0056027425, -0.0156039, 0.06932739, 0.045712095, -0.0005207572, -0.010891313, 0.018261276, 0.006728527, 0.052754797, -0.03296193, -0.02440073, 0.093204506, 0.019517966, -0.026770113, -0.05388058, -0.0012632352, 0.024505453, -0.018274367, -0.015185003, 0.021049555, 0.0139806755, 0.04707351, -0.31103075, 0.050503228, 0.06608094, -0.072469115, 0.05843608, 0.02417819, 0.03602511, -0.0023382942, -0.02263351, -0.02417819, -0.00091306376, -0.022319337, 0.010321875, -0.027987532, -0.023327306, -0.043957967, 0.004863128, 0.046759337, 0.02590614, 0.012625807, -0.009104457, 0.0057892823, 0.0011396934, -0.05084358, -0.00541293, -0.019688142, 0.19080742, 0.11980444, -0.014582839, -0.019256154, 0.060530566, 0.03929774, -0.09037695, -0.14745162, 0.038355224, 0.07372581, -0.023864018, 0.02544797, -0.0058841887, -0.010341511, 0.034428068, 0.0020715748, 0.029636938, -0.060844738, 0.015224275, -0.033799723, -0.029794024, 0.0049580345, -0.014386482, 0.034061532, 0.0070950617, -0.070845895, 0.007350327, 0.042177655, 0.0030451822, -0.004172603, -0.025303975, -0.05445656, 0.0079852175, 0.022960773, -0.017331848, 0.019413242, -0.02038194, -0.051995546, -0.0048107663, 0.05265007, -0.027149739, -0.064876616, 0.012429449, -0.01636315, -0.06288686, -0.008692105, -0.009889888, -0.08152776, 0.03275248, 0.03772688, 0.010550959, -0.0016968587, -0.08482657, 0.028327886, 0.019688142, -0.0019259427, 0.01586571, -0.004748586, 0.005651832, 0.0229215, -0.037334163, -0.010118972, 0.014190123, -0.037124716, -0.049743976, 0.032621577, -0.04652371, -0.07095062, -0.021088827, -0.04479576, -0.35040703, 0.027620997, 0.011918918, 0.033276103, -0.046445165, 0.060216393, 0.0049907607, 0.06602858, -0.06445772, 0.02589305, -0.04406269, -0.017567478, 0.032255042, 0.066866376, 0.010354602, 0.016140612, -0.003828977, -0.07388289, 0.0053540226, 0.011657109, 0.026233403, -0.0034951689, 0.13635086, -0.014373391, 0.0025281068, 0.012521083, -0.032595396, 0.00516421, 0.030370006, -0.04154931, 0.04181112, -0.015891891, 0.037805423, 0.0104265995, -0.020578297, 0.014779197, 0.008521928, 0.025251614, 0.03955955, 0.044612493, -0.076448634, -0.020604478, 0.016899861, -0.0372818, 0.053828217, 0.03777924, 0.013286877, -0.05513727, 0.016965315, -0.022712052, 0.01786856, 0.0032219042, 0.028249342, 0.031155437, 0.04628808, -0.0006549351, 0.008652833, 0.013195245, -0.011486932, -0.02542179, -0.03804105, -0.066133305, 0.03900975, -0.012599626, 0.0127894385 ]
Structure of taq DNA polymerase shows a new orientation for the structure-specific nuclease domain.
e domain is too far from that of the polymerase domain; making it difficult to propose a structural model for the in vivo primer-excision and nick-translation activities of the enzyme. In the present structure; the two active sites are considerably closer. Taken together; the reported structure of the native enzyme; that of the Fab complex and the present structure imply that the different orientation of the structure-specific nuclease domain is probably a consequence of intrinsically high relative mobility
10666572
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0.0372059, -0.014903575, -0.017847164, 0.009506996, -0.0003890808, -0.023044853, -0.07345712, -0.0012629586, 0.020923346 ]
Structure of taq DNA polymerase shows a new orientation for the structure-specific nuclease domain.
between these two domains in this enzyme.
10666572
[ 0.0013786216, -0.0056342217, 0.02298922, 0.011361571, 0.091371514, -0.04196065, -0.05938882, 0.010057785, -0.005128672, 0.051645923, 0.06886123, -0.017108876, 0.059920978, 0.04334426, -0.06380573, 0.03903378, -0.006578802, -0.04060365, -0.020514688, 0.02274975, 0.05183218, -0.05928239, -0.035069205, -0.04539307, 0.05209826, 0.029029213, -0.015818393, -0.05550407, -0.033233263, -0.18689385, -0.006359287, 0.010942497, 0.029481547, -0.019969225, -0.0272997, -0.038528234, -0.0026341816, 0.011893729, -0.1189905, 0.03448383, 0.0010002905, 0.04334426, -0.039539333, 0.009153116, -0.05789878, -0.004819355, -0.009785053, -0.01732174, 0.029747626, 0.0013769586, -0.04198726, -0.016470287, -0.0475217, 0.025357325, 0.011521218, 0.030386217, 0.0074102986, 0.04033757, -0.0026857343, -0.009731838, 0.026035825, 0.040364176, -0.0980767, -0.008062192, 0.07503426, 0.020009138, 0.023720939, -0.030066922, -0.028975997, -0.0009670307, -0.013350511, -0.014048968, 0.041135807, 0.000636095, 0.0013046183, 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Structure of agkistrodotoxin in an orthorhombic crystal form with six molecules per asymmetric unit.
The structure of agkistrodotoxin crystallized under basic conditions has been determined at 2.8 A resolution by the molecular-replacement technique and refined to a crystallographic R factor of 0.194 and a free R factor of 0.260 with good stereochemistry. The molecular packing in the crystal differs from other PLA(2)s. The six molecules in the asymmetric unit form three dimers linked by Ca(2+) ions in a near-perfect six-ligand octahedral coordinating system. Extensive intermolecular hydrophobic interactions
10666574
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Structure of agkistrodotoxin in an orthorhombic crystal form with six molecules per asymmetric unit.
occur at the interfacial recognition site of each neurotoxin molecule; which provides an insight into phospholipase A(2)-membrane interactions. This hydrophobic interaction-induced molecular association along the interfacial recognition site suggests a self-protection mechanism of agkistrodotoxin.
10666574
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0.0011219704, -0.04499849, 0.007985105, -0.010491669, 0.0069146617, -0.064306356, 0.019174889, 0.042950686, 0.04417405, -0.025517762, 0.07255076, 0.0020012627 ]
Comparing anisotropic displacement parameters in protein structures.
The increasingly widespread use of synchrotron-radiation sources and cryo-preparation of samples in macromolecular crystallography has led to a dramatic increase in the number of macromolecular structures determined at atomic or near-atomic resolution. This permits expansion of the structural model to include anisotropic displacement parameters U(ij) for individual atoms. In order to explore the physical significance of these parameters in protein structures; it is useful to be able to compare quantitativel
10666575
[ -0.051674083, -0.022486072, 0.030158728, -0.03452031, 0.013144578, -0.03148848, 0.069625705, 0.06744491, -0.055530358, -0.017805351, 0.00803169, -0.091699556, -0.0031947242, 0.010225777, -0.028057724, -0.059838746, -0.043216873, 0.025065785, -0.0117815845, -0.013629937, -0.009275006, -0.057338815, 0.012167212, -0.06654069, 0.029999157, 0.07021079, 0.038828697, 0.021262702, -0.038057443, -0.19488814, 0.01121644, -0.0065323967, -0.066008784, -0.030451274, -0.027113602, 0.034413926, -0.01866969, -0.033509698, -0.012785546, 0.10542257, 0.005412082, -0.001073773, -0.011648609, -0.0052757827, 0.0781893, -0.028802384, -0.062232297, -0.01982657, 0.08345511, -0.014387894, -0.017326642, 0.04111587, 0.0026594999, 0.004630854, 0.026727973, -0.0014261568, 0.046115726, 0.109784156, 0.026794462, -0.023430193, 0.015983595, 0.063296095, -0.09632708, 0.04098289, 0.054626126, -0.027206684, 0.005029779, 0.042977516, 0.036036223, 0.009926584, -0.015371909, -0.015398504, 0.004860236, -0.0049998597, 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-0.033775646, 0.017885137, -0.049945407, 0.047631644, 0.031142743, -0.0010122721, -0.0457434, -0.025597686, 0.020797288, 0.08217855, 0.030903388 ]
[ -0.05164461, -0.022498114, 0.030210234, -0.034438603, 0.013190384, -0.031433538, 0.069621824, 0.06749434, -0.05558045, -0.017791063, 0.007991351, -0.09174763, -0.003192884, 0.010265097, -0.02805616, -0.05983541, -0.043161277, 0.025011202, -0.011834115, -0.013669067, -0.009221301, -0.057229247, 0.01217983, -0.06653698, 0.03002408, 0.07020688, 0.038826533, 0.021221627, -0.038002133, -0.19498366, 0.011249057, -0.0065120873, -0.06605829, -0.030502763, -0.02715198, 0.034438603, -0.018681945, -0.033587612, -0.012811426, 0.10552307, 0.005451671, -0.0010230193, -0.011641311, -0.005238923, 0.07813175, -0.028827371, -0.06222883, -0.019812169, 0.08345045, -0.014387093, -0.01735227, 0.041166764, 0.0026394064, 0.004613975, 0.026713187, -0.0014053012, 0.04613975, 0.10977803, 0.026806263, -0.023388997, 0.015996, 0.06323938, -0.09632172, 0.04092742, 0.054569896, -0.027205167, 0.0049929325, 0.043001715, 0.036060806, 0.009945975, -0.015357755, -0.015357755, 0.0048699374, -0.00494307, 0.012193127, 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-0.049889434, 0.047628988, 0.03108782, -0.0010221882, -0.045714255, -0.025582962, 0.020769536, 0.082173966, 0.030901665 ]
Comparing anisotropic displacement parameters in protein structures.
y the electron-density distribution described by the refined U(ij) values associated with corresponding crystallographically independent atoms. This paper presents the derivation of an easily calculated correlation coefficient in real space between two atoms modeled with anisotropic displacement parameters. This measure is used to investigate the degree of similarity between chemically equivalent but crystallographically independent atoms in the set of protein structural models currently available from the
10666575
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Comparing anisotropic displacement parameters in protein structures.
Protein Data Bank.
10666575
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Three-centre C-H---O hydrogen bonds in the DNA minor groove: analysis of oligonucleotide crystal structures.
AA.TT and GA.TC dinucleotide steps in B-DNA-type oligomeric crystal structures and in protein-bound DNA fragments (solved using data with resolution <2.6 A) show very small variations in their local dinucleotide geometries. A detailed analysis of these crystal structures reveals that in AA.TT and GA.TC steps the electropositive C2-H2 group of adenine is in very close proximity to the keto O atoms of both the pyrimidine bases in the antiparallel strand of the duplex structure; suggesting the possibility of i
10666576
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Three-centre C-H---O hydrogen bonds in the DNA minor groove: analysis of oligonucleotide crystal structures.
ntra-base pair as well as cross-strand inter-base pair C-H---O hydrogen bonds in the DNA minor groove. The C2--H2---O2 hydrogen bonds in the A.T base pairs could be a natural consequence of Watson-Crick pairing. However; the cross-strand interactions between the bases at the 3'-end of the AA.TT and GA.TC steps obviously arise owing to specific local geometry of these steps; since a majority of the H2---O2 distances in both data sets are considerably shorter than their values in the uniform fibre model (3.3
10666576
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0.05160999, 0.004091687, -0.07374381, -0.02880868, -0.030116951, -0.005636916, -0.007242219, 0.03163882, -0.066054374, 0.029930055, 0.03107813, 0.08036527, 0.015018427, 0.03353448, 0.02181343, 0.049073543, -0.0000017208614, 0.011080261, -0.015712611, 0.026806222, -0.01345651, -0.28109154, 0.011981367, 0.033133987, 0.051129397, -0.01943718, 0.005947297, 0.023415396, -0.0077428333, -0.010132432, -0.007482514, 0.015365519, 0.027220063, 0.036871906, 0.028408188, -0.016580343, 0.055855196, 0.072836034, -0.054840617, 0.0036678335, -0.04771187, -0.028968876, -0.057724155, 0.1671384, 0.009211302, 0.031425223, 0.05246437, 0.008597215, 0.08009827, -0.029422766, -0.0030036853, -0.03537674, 0.027059866, 0.043973953, 0.02744701, -0.042078294, 0.002720004, -0.014924979, -0.00997891, 0.042959373, -0.031692218, -0.04130401, 0.012789024, -0.015552415, -0.022787958, 0.05895233, -0.09216642, -0.002065868, -0.060073707, -0.07833611, -0.015872808, -0.021733332, 0.068884514, 0.038126778, -0.00032373052, -0.036978703, 0.011707698, 0.018863143, 0.009418222, 0.03532334, -0.031718917, 0.03863407, 0.0016395116, -0.00486597, 0.12879802, 0.00810995 ]
Three-centre C-H---O hydrogen bonds in the DNA minor groove: analysis of oligonucleotide crystal structures.
A) and many are even smaller than the sum of the van der Waals radii. The analysis suggests that in addition to already documented features such as the large propeller twist of A.T base pairs and the hydration of the minor groove; these C2-H---O2 cross-strand interactions may also play a role in the narrowing of the minor groove in A-tract regions of DNA and help explain the high structural rigidity and stability observed for poly(dA).poly(dT).
10666576
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-0.007702693, 0.02969521, -0.017955244, 0.08377343, 0.045366205, -0.010358795, -0.01630846, -0.0060990723, -0.041674227, 0.039044686, 0.02836716, -0.01738418, 0.006958985, -0.043480374, 0.048845697, 0.08191416, -0.029456161, -0.04948316, 0.0127891265, 0.023028396, -0.028818697, 0.044011593, 0.002941632, 0.053786047, -0.032563798, 0.11484981, 0.04865977, -0.03131543, 0.0036222578, -0.0036521389, 0.078514345, -0.058434222, -0.05731866, -0.0063680024, 0.0077358945, -0.0059596268, -0.017238095, 0.041780468, 0.010040062, 0.019641867, 0.026600853, -0.03415746, -0.08334845, -0.030252991, -0.017968524, 0.017264657, 0.041700788, 0.059549786, 0.048128553, 0.005103034, -0.057956126, 0.0629496, 0.0316076, 0.016667034, -0.007231235, -0.011779808, 0.0061654747, 0.046136476, -0.004790942, 0.023028396, -0.026587572, -0.025100155, 0.0060525904, -0.018021645, 0.037743196, 0.008625688, -0.00029383117, 0.065127596, -0.012862169, 0.005644215, 0.052882973, -0.047172356, -0.007543327, 0.019774672, 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-0.021979237, -0.008121029, -0.031049822, 0.013499633, -0.027025828, 0.041222688, 0.008758494, 0.0039741914, -0.029642088, 0.053493876, 0.038965 ]
[ -0.08813059, -0.037159342, -0.01816797, 0.006348165, 0.05065251, -0.02014679, 0.07639047, 0.031209597, -0.037265588, 0.022006087, 0.0183539, -0.055725735, 0.034609452, -0.024104433, -0.036415625, -0.004505471, -0.01035229, 0.011620595, -0.042737227, -0.04456996, 0.092858516, -0.02382554, 0.012530321, -0.09663023, 0.04961662, 0.026441833, -0.02128893, 0.014993887, -0.02108972, -0.25583902, 0.005690771, -0.02831441, 0.012032296, -0.05391956, -0.051635284, 0.0068860324, -0.02070458, -0.002168071, -0.041541968, 0.061356742, 0.03901864, 0.0028669669, 0.003280328, 0.004937093, 0.04863385, -0.033148576, -0.05296335, 0.026614483, 0.08127776, -0.045499608, 0.0028719471, -0.001875896, 0.023984907, 0.037451517, -0.027570691, -0.012523681, 0.037185904, 0.007656312, -0.00040381568, 0.008499635, 0.03907176, -0.009296476, -0.09742707, 0.059656814, 0.029031565, 0.04589803, 0.014927484, -0.024834871, 0.040001407, 0.03514068, -0.011554192, 0.070068866, -0.016082903, 0.0025648314, -0.013772065, 0.035964083, -0.01873904, 0.009708177, 0.03142209, 0.0171852, 0.012782655, 0.028872197, 0.011109289, -0.024130996, -0.049935356, 0.02522001, 0.027491007, 0.010465176, 0.04685424, 0.0040771686, 0.05192746, -0.040320143, -0.0013620998, -0.02111628, -0.103429936, 0.0031541614, 0.017211761, -0.020930352, -0.0046382775, 0.4398561, -0.06831582, 0.004528712, -0.017357849, 0.06560656, -0.0042896597, -0.040771686, -0.014781397, -0.025405942, -0.0016376738, 0.03516724, 0.06677526, -0.012961944, -0.030997107, 0.007344216, -0.002304198, -0.051396232, 0.0019788214, -0.03182051, -0.04496838, 0.084890105, -0.023984907, 0.04472933, 0.013533013, 0.01191277, 0.011281937, -0.011155771, -0.038381167, 0.10066755, 0.054211736, 0.0014492542, 0.015485273, 0.050466582, -0.005647609, -0.03580471, -0.012922102, 0.025073923, 0.029562794, 0.002012023, -0.0027358201, -0.02225842, -0.022696681, -0.027836306, -0.0078156805, -0.05075876, -0.061622355, 0.027278516, -0.002481827, 0.0480495, -0.0065971776, 0.04807606, 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0.029669039, -0.0179422, 0.08377453, 0.045393363, -0.010358931, -0.016361797, -0.0061223935, -0.041648213, 0.039098322, 0.028367532, -0.017410971, 0.0069457954, -0.043480948, 0.04884634, 0.08196836, -0.029350303, -0.049457252, 0.012789295, 0.023015419, -0.028845636, 0.043985613, 0.0029549513, 0.053839877, -0.032564227, 0.11485132, 0.04860729, -0.031342406, 0.0036355862, -0.003555902, 0.0785685, -0.058488116, -0.057319414, -0.0063514854, 0.0076695927, -0.0059663453, -0.017251603, 0.04180758, 0.010060115, 0.019668687, 0.026641045, -0.03418447, -0.08334955, -0.030333074, -0.0179422, 0.017238323, 0.041727897, 0.059497446, 0.048129182, 0.005059939, -0.057956886, 0.062950425, 0.031581458, 0.016693816, -0.007171567, -0.011846366, 0.006132354, 0.046163645, -0.004797646, 0.023015419, -0.026561359, -0.025060643, 0.0060991524, -0.018035164, 0.037770253, 0.008605881, -0.00028242197, 0.06512845, -0.012782655, 0.00567085, 0.05293679, -0.047226097, -0.007523505, 0.019774932, 0.02111628, -0.012005734, -0.03474226, -0.07150318, 0.036150012, -0.022988858, -0.00068354, 0.054371104, -0.033547, 0.01795548, -0.0015936816, 0.01600322, -0.02363961, 0.03373293, -0.0009860905, 0.0018825363, -0.027809743, -0.040612318, -0.007251251, 0.032936085, -0.01054486, -0.27793807, 0.013154513, -0.006155595, 0.043454386, -0.076815456, 0.08175587, 0.03968267, -0.051236864, -0.0010956561, -0.004415826, -0.009416002, 0.059444323, 0.060453653, 0.04555273, -0.036176573, 0.0066170986, 0.05118374, 0.0004627487, -0.02089051, -0.018606232, 0.0053056316, -0.033493876, 0.12823825, 0.03710622, -0.01856639, -0.03612345, 0.009900747, -0.039337374, -0.06730649, 0.048952587, -0.05192746, 0.0187656, 0.045021504, -0.03144865, -0.0060360692, 0.07097195, 0.030837739, -0.044596523, 0.010385492, -0.03373293, -0.008878134, -0.025644993, -0.076337345, -0.09052111, 0.03160802, -0.08828996, 0.0054550394, 0.01660085, -0.022842769, -0.014382976, -0.04318877, -0.014688432, -0.03166114, -0.029536232, -0.021966245, -0.008141057, -0.031103352, 0.013519732, -0.026999623, 0.041302916, 0.008758608, 0.003980884, -0.029642478, 0.05346802, 0.038992077 ]
Human apolipoprotein A-I: structure determination and analysis of unusual diffraction characteristics.
The crystallization and structure determination of recombinant human apolipoprotein A-I (apo A-I); the major protein component of high-density lipoprotein; is described. The fragment crystallized; residues 44-243 of native apo A-I [apo Delta(1-43)A-I]; is very similar to intact native apo A-I in its ability to bind lipid; to be incorporated into high-density lipoproteins and to activate lecithin-cholesterol acyl transferase. Apo Delta(1-43)A-I crystallizes from 1.0-1.4 M sodium citrate pH 6.5-7.5 in space g
10666577
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Human apolipoprotein A-I: structure determination and analysis of unusual diffraction characteristics.
roup P2(1)2(1)2(1); with unit-cell parameters a = 97.47; b = 113.87; c = 196.19 A (crystal form I). The crystals exhibit unusual diffraction intensity spikes and axial extinctions that are discussed in the context of the 4 A crystal structure. When flash-cooled to 100 K; the crystals diffract synchrotron radiation to 3 A resolution. Radiation sensitivity and crystal-to-crystal variation have hindered the assembly of a complete 3 A data set.
10666577
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X-ray diffraction of helices with arbitrary periodic ligand binding.
The classical formalism for studying diffraction from helical structures extended to include ligand binding is presented. The diffraction from such a binding pattern is the convolution of the Fourier transforms of the helix and the one-dimensional binding distribution. It is shown in the present analysis that it is not necessary to assume that the binding distribution is strictly periodic; as long as its Fourier transform can be determined. Analysis of the convolution gives a general expression for the diff
10666578
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0.020912766, -0.0201171, -0.03604369, 0.009906047, -0.030023148, 0.013990468, 0.0005482639, -0.027768759, 0.036494568, 0.036494568, -0.021138206, 0.06513856, 0.024758488 ]
X-ray diffraction of helices with arbitrary periodic ligand binding.
racted intensities and the selection rule for the layer-lines. It shows two groups of layer-lines: one group is the familiar layer-line set from the original helix; while the other group shows reciprocal spacings shifted by 1/a from the original helix layer-lines; where a is the average repeat of the binding distribution. This group of layer-lines is contributed by the ligand only. By way of examples; calculated diffraction patterns from muscle actin filaments with bound myosin heads in three different bind
10666578
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0.022444457, -0.0403713, -0.052070096, -0.016764795, -0.04324377, -0.04507171, -0.0046220697, -0.008800212, 0.029038088 ]
X-ray diffraction of helices with arbitrary periodic ligand binding.
ing patterns are presented. This approach provides a method for determining the ligand-binding distribution along helices by an analysis of their X-ray diffraction patterns.
10666578
[ -0.051101208, 0.02606987, 0.00089040986, 0.008075269, 0.038905088, 0.016896151, -0.027135033, 0.024685157, 0.0394643, 0.013940324, 0.026455991, 0.017015982, -0.0027810747, -0.024179205, -0.008774282, -0.008880799, 0.0064342516, 0.00079387944, 0.000020999007, 0.025444087, 0.031502202, -0.04210058, 0.09181707, 0.01973215, 0.03179512, 0.0021569557, -0.032247815, -0.013966952, -0.006347707, -0.19354016, -0.0515539, -0.0064076227, -0.006447566, -0.0027660958, 0.012855189, 0.017055927, -0.0018923291, 0.0010884637, -0.014645995, -0.0047932346, 0.008294959, 0.0336059, 0.00016216694, -0.05150064, -0.0044470564, 0.030916363, -0.03246085, -0.014153357, 0.06422934, -0.042926077, 0.004353855, 0.009040573, -0.0059715714, 0.05213974, -0.016230425, 0.003316985, 0.0044836714, 0.029371876, -0.006141332, 0.038638797, 0.03560308, 0.05035559, -0.1976943, 0.014739196, 0.054749392, 0.012262692, -0.022408372, -0.07093987, 0.0032886914, 0.014992173, -0.021742644, 0.011457162, 0.025989983, -0.033978708, 0.027001888, -0.016004078, -0.0013689012, 0.017934686, 0.001975545, -0.011763397, 0.029584909, 0.010092421, 0.014699252, -0.03941104, -0.0298512, -0.005528863, 0.06907584, -0.021423096, -0.00035449964, 0.0074761147, 0.046760667, -0.0037547003, 0.08191105, 0.05879701, -0.06273811, 0.028892552, 0.056400392, 0.007942123, -0.03368579, 0.49508786, -0.047160104, 0.03815947, 0.019013165, 0.08372183, -0.019079736, -0.017548565, -0.0074028843, -0.04375158, -0.02782739, 0.058370944, 0.028546374, -0.004130836, 0.017814854, -0.020610908, 0.039198007, -0.010165651, 0.061939243, 0.027254865, -0.017814854, 0.022182025, -0.032966804, 0.0049763094, 0.061885983, 0.016563289, -0.003202147, 0.0425799, -0.029691424, 0.08244363, 0.016123908, 0.04777257, 0.045855276, -0.03504387, 0.011596965, -0.046121567, -0.0025347557, -0.021383151, -0.011190871, 0.021596184, 0.028759407, -0.047639426, 0.007043392, -0.026109815, -0.09181707, -0.009579812, -0.015604641, 0.09858086, -0.0313158, 0.026429363, -0.043032594, 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-0.30889735, -0.064548895, -0.02231517, -0.06050127, -0.01109767, -0.037174195, 0.012588898, 0.024472125, -0.066838995, 0.08920742, -0.038292617, 0.02287438, -0.057572074, 0.002809368, -0.009479953, 0.0071965093, -0.009160404, -0.03911812, 0.011237472, 0.004533601, 0.009599783, 0.030729959, -0.08244363, 0.029265359, 0.01580436, 0.03211467, 0.13186722, 0.09229639, -0.027854018, 0.006141332, -0.020650852, 0.024991393, 0.03445803, -0.03887846, -0.024844933, 0.008847512, -0.023806399, -0.026189702, 0.039863735, -0.012808588, -0.0029125558, 0.019492486, 0.0010867993, 0.025723692, -0.010119051, -0.0070567066, -0.004916394, 0.026282903, -0.027987164, 0.045083035, 0.0064508948, -0.010045821, 0.0082883015, 0.04289945, -0.024671843, -0.017748283, -0.10358712, -0.01750862, 0.0027294809, 0.05783836, 0.007615917, -0.0051327553, 0.020504393, -0.029451763, -0.017002668, -0.015870932, -0.033659156, 0.016390199, 0.05299187, 0.003711428, -0.007782349, 0.10326757, -0.03815947, -0.014792454, -0.021529611, 0.027587729, 0.032247815, -0.072857164, -0.007962096, 0.026895372, 0.009992562, 0.0086145075, 0.0063144206, 0.04899751, 0.0037780008, 0.06593361, -0.026948629, -0.020051697, -0.05714601, 0.008301616, -0.018453954, 0.02228854, -0.0032803698, 0.066146635, 0.034963984, 0.030303894, -0.2577695, -0.0156579, 0.060980596, 0.008674423, 0.039916992, 0.03041041, -0.081538245, -0.02085057, 0.005938285, 0.01853384, -0.00860785, 0.09336156, 0.008261672, -0.021542927, -0.045855276, 0.017055927, -0.006777101, -0.02029136, 0.016350256, -0.026189702, 0.032860287, -0.021782588, 0.13133463, -0.059010044, -0.027108405, 0.04380484, -0.004377155, -0.0008820883, -0.03254074, -0.034777578, 0.061513178, -0.016549973, 0.016749691, 0.011923171, -0.023300447, 0.009207005, -0.03179512, -0.033632528, 0.042979337, -0.014765825, 0.014086784, -0.034005336, -0.0086145075, -0.02475173, 0.048491556, 0.013048249, -0.059169818, -0.06502821, -0.013094851, -0.0029425134, -0.038479023, -0.029265359, 0.041621253, 0.03272714, -0.056400392, 0.023406962, -0.018520527, -0.022847751, -0.032247815, -0.032886915, -0.008394818, -0.025444087, -0.027987164, 0.040422946, 0.023912914 ]
[ -0.051098935, 0.026055397, 0.0009211588, 0.008121508, 0.038903356, 0.016908715, -0.027067257, 0.024697375, 0.039409287, 0.013939704, 0.02646813, 0.016975284, -0.0027975934, -0.024191445, -0.00880052, -0.008893717, 0.006477236, 0.0007867711, 0.0000074045834, 0.025469583, 0.03152743, -0.042072076, 0.09197275, 0.019757899, 0.03182034, 0.0021135893, -0.03227301, -0.013939704, -0.006397352, -0.19353156, -0.051578235, -0.0063840384, -0.0064472794, -0.0027693012, 0.012854617, 0.017135052, -0.0019188728, 0.0010817583, -0.014645343, -0.0048196493, 0.008281276, 0.03368429, 0.00010838386, -0.051471725, -0.0044368734, 0.030914988, -0.032486033, -0.014126099, 0.064226486, -0.042977426, 0.004320376, 0.008986915, -0.0059513347, 0.052190676, -0.016296273, 0.0032835526, 0.0045101, 0.029343942, -0.0061344015, 0.03863708, 0.035601497, 0.05037998, -0.19768551, 0.014738541, 0.0546937, 0.012235519, -0.022407375, -0.07093672, 0.0032302968, 0.015031448, -0.02178162, 0.011430025, 0.026015455, -0.033950567, 0.026987374, -0.015990052, -0.0013388839, 0.017960517, 0.0020120705, -0.01176953, 0.029556965, 0.010091973, 0.014685285, -0.039435916, -0.029903129, -0.005505318, 0.06907276, -0.021422142, -0.0003245275, 0.0075356946, 0.046758585, -0.0037545334, 0.08185416, 0.058794394, -0.06273533, 0.02886464, 0.05634463, 0.007915142, -0.033737544, 0.49506587, -0.047158007, 0.038131148, 0.018999005, 0.08366485, -0.019105516, -0.017521156, -0.007375927, -0.043749634, -0.027799524, 0.05836835, 0.028545106, -0.004127324, 0.017827377, -0.020663248, 0.039169636, -0.0101652, 0.061883233, 0.027293595, -0.017814063, 0.022234295, -0.032938708, 0.0050060446, 0.061936487, 0.016549237, -0.003246939, 0.042684518, -0.029690105, 0.08249322, 0.016136505, 0.047770448, 0.04585324, -0.035042312, 0.011636391, -0.04611952, -0.0025462927, -0.021289004, -0.011190373, 0.021661794, 0.0287315, -0.047637306, 0.0070164506, -0.026121967, -0.09181299, -0.009599357, -0.015630575, 0.09862973, -0.03139429, 0.026454816, -0.043004055, 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0.02761313, 0.032219756, -0.07296044, -0.007975055, 0.026960745, 0.010025403, 0.008640752, 0.006294169, 0.048968703, 0.0037545334, 0.06593067, -0.027000688, -0.01999755, -0.05709021, 0.008327874, -0.01841319, 0.022247607, -0.0032852169, 0.0661437, 0.034909174, 0.030302547, -0.25775805, -0.015630575, 0.06087137, 0.008667381, 0.039861962, 0.030409059, -0.08164113, -0.02083633, 0.0059213787, 0.01854633, -0.008580839, 0.09341066, 0.008307904, -0.021528654, -0.045879867, 0.01702854, -0.006723544, -0.020290457, 0.016336214, -0.026188536, 0.03288545, -0.021821562, 0.13132879, -0.059007417, -0.027133826, 0.043749634, -0.004386946, -0.00087039935, -0.03253929, -0.03480266, 0.06151044, -0.01658918, 0.016695691, 0.011909327, -0.023272783, 0.009226566, -0.03179371, -0.033604406, 0.042977426, -0.0146985985, 0.014032901, -0.03392394, -0.008567526, -0.024777258, 0.04846277, 0.013047669, -0.05911393, -0.06502532, -0.013174152, -0.0029274044, -0.038530566, -0.029264059, 0.041592773, 0.032699056, -0.056397885, 0.023512432, -0.01854633, -0.022873363, -0.03227301, -0.03288545, -0.008321217, -0.0253897, -0.028012548, 0.040421147, 0.023938479 ]
Expression, purification, crystallization and preliminary X-ray analysis of Escherichia coli argininosuccinate synthetase.
A recombinant form of Escherichia coli argininosuccinate synthetase with a C-terminal polyhistidine affinity tag has been expressed; purified and subsequently crystallized using the hanging-drop vapour-diffusion technique. The crystals grow as large rectangular chunks with unit-cell dimensions a = 79.70; b = 105.84; c = 127.33 A; alpha = beta = gamma = 90 degrees. The crystals exhibit the symmetry of space group I222 and diffract to a minimum d-spacing of 1.6 A at station X8C of the National Synchrotron Lig
10666579
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-0.06323064, 0.0056575136, 0.04050713, 0.016021278, 0.023270907, -0.007930532, 0.067930214, -0.01655532, -0.10200214, 0.077649795, 0.029933088 ]
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-0.035675682, 0.009412932, 0.06034958, -0.033218972, 0.03065545, 0.025982363, -0.019880647, 0.03383315, -0.002480074, 0.03177699, 0.0051804506, -0.04355317, 0.043579873, 0.0030708858, 0.017463993, 0.018972732, 0.07957599, -0.024940932, -0.04958813, 0.0035248427, 0.028839622, -0.26959705, 0.01265739, 0.04339295, 0.005901441, -0.035008095, -0.040962946, -0.019066194, -0.06301992, -0.0027103904, 0.012296895, -0.012717472, 0.0070964163, 0.03201732, -0.0133850565, -0.007483615, 0.01560811, 0.0859848, -0.06990938, -0.0010656307, -0.07535686, -0.0549555, -0.045422405, 0.12871017, 0.03150996, 0.017210312, 0.06852081, -0.01966702, -0.0054274565, -0.08689272, 0.045155372, 0.030788967, -0.031830397, -0.0045662737, 0.019573558, 0.027531158, 0.051804505, -0.007677214, 0.00090374163, -0.06857421, -0.031189518, -0.07904193, 0.054287918, -0.019920701, 0.0334326, 0.08320765, -0.0406158, 0.0051504094, -0.052845936, -0.027317531, 0.023685874, -0.010454363, 0.008478315, 0.028839622, -0.06067002, -0.06318013, 0.005661111, 0.040428877, 0.01600866, 0.023298677, -0.007937572, 0.06793333, -0.016529376, -0.1019534, 0.077653356, 0.02993446 ]
Expression, purification, crystallization and preliminary X-ray analysis of Escherichia coli argininosuccinate synthetase.
ht Source; Brookhaven National Laboratory. On the basis of density calculations; one monomer of this homotetrameric protein is predicted per asymmetric unit (Matthews coefficient V(m) = 2.69 A(3) Da(-1)).
10666579
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Crystallization and preliminary analysis of bovine adenosine deaminase.
Adenosine deaminase (ADA) from bovine intestine was crystallized with purine riboside by vapour diffusion using ammonium sulfate as precipitant. The crystals are tetragonal and have unit-cell parameters a = b = 80.03; c = 141.68 A. They belong to space group P4(1)2(1)2 or P4(3)2(1)2 and diffract to at least 2.0 A resolution. The structure is being solved by molecular replacement.
10666580
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Crystallization and preliminary X-ray analysis of the Escherichia coli UDP-MurNAc-tripeptide D-alanyl-D-alanine-adding enzyme (MurF).
Crystals of the Escherichia coli UDP-MurNAc-tripeptide D-Ala-D-Ala-adding protein (MurF); which catalyzes the formation of the last metabolite of the bacterial cell-wall building block; have been grown in hanging-drop vapor-diffusion trials using PEG 8K as a precipitating agent. The crystals belong to hexagonal space group P6(1) or P6(5); with unit-cell dimensions a = b = 74; c = 425 A. The asymmetric unit contains two molecules; with a crystal volume per protein mass (V(m)) of 3.4 A(3) Da(-1) and a solvent
10666581
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0.029539526, 0.016354617, 0.031164333, 0.023386568, 0.047678765, -0.011819806, -0.0043217205, 0.09999223, -0.062062304, 0.04757222, 0.01904487 ]
Crystallization and preliminary X-ray analysis of the Escherichia coli UDP-MurNAc-tripeptide D-alanyl-D-alanine-adding enzyme (MurF).
content of about 64% by volume. A native data set to 2.8 A resolution has been obtained from a frozen crystal using a synchrotron X-ray source.
10666581
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0.05943443, 0.0428629, 0.027539544, -0.020355893, 0.035878424, 0.046554312, -0.02011688, 0.07473122, 0.018802311 ]
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0.0054371376, 0.018628336, 0.059430104, 0.042886335, 0.027590651, -0.020354412, 0.03584926, 0.046550926, -0.020168528, 0.074725784, 0.018854054 ]
Crystallization and preliminary X-ray analysis of birch-pollen allergen Bet v 1 in complex with a murine monoclonal IgG Fab' fragment.
The human type I allergic response is characterized by the presence of allergen-specific serum immunoglobulin E (IgE). Allergen-mediated cross-linking of receptor-bound IgE on the surface of mast cells and circulating basophils triggers the release of mediators; resulting in the development of the clinical symptoms of allergy. In order to study the structural basis of allergen-antibody interaction; a complex between the major birch-pollen allergen Bet v 1 and a Fab' fragment isolated from the murine monoclo
10666582
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0.04010874, 0.05328236, -0.032038894, 0.029767578, 0.066268936, -0.04940777, 0.07968305, 0.00596554 ]
Crystallization and preliminary X-ray analysis of birch-pollen allergen Bet v 1 in complex with a murine monoclonal IgG Fab' fragment.
nal Bet v 1 antibody BV16 has been crystallized. Complex crystals belong to space group P1; with unit-cell parameters a = 91.65; b = 99.14; c = 108.90 A; alpha = 105.7; beta = 98.32; gamma = 97.62 degrees; and diffract to 2.9 A resolution when analyzed at 100 K using synchrotron-generated X--rays.
10666582
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Ethylammonium nitrate: a protein crystallization reagent.
Ethylammonium nitrate (EAN) is a liquid organic salt that has many potential applications in protein chemistry. Because this solvent has hydrophobic and ionic character as well as the ability to hydrogen bond; it is especially well suited for broad use in protein crystallography. For example; EAN may be used as an additive; a detergent; a precipitating agent or to deliver ligands into protein crystals. A discussion of the crystallization of lysozyme using EAN as a precipitating agent is given here.
10666583
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Structural studies of the Msx-1 homeodomain-DNA complex I.
Crystals of the Msx-1 homeodomain-DNA complex have been obtained by hanging-drop vapor diffusion at 293 K in 12% PEG 4000 and 0.1 M sodium acetate pH 4.6. The homeodomain consists of 60 amino acids and is the DNA-binding domain. The DNA in the complex was 16 base pairs with the sequence 5'-TGTCACTAATTGAAGG-3'; containing an overhang T at each end. The crystals diffract to 2.15 A (99.8% completeness) using cryogenic (123 K) conditions. The crystals belong to the orthorhombic space group P2(1)2(1)2(1); with u
10666584
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Structural studies of the Msx-1 homeodomain-DNA complex I.
nit-cell parameters a = 33.66; b = 60.96; c = 83.37 A. The structure will illuminate the details of Msx-1-DNA binding specificity and clarify its role in transcriptional regulation. Mutations in Msx-1 cause craniofacial deformities in mice.
10666584
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Crystallization and preliminary X-ray diffraction studies of Streptococcus pyogenes plasmid pSM19035-encoded omega transcriptional repressor.
The transcriptional repressor; omega protein; from the Streptococcus pyogenes broad-host-range plasmid pSM19035 was crystallized at pH 7. 5 and 8.5 by the vapour-diffusion method using PEG 4000 as precipitant. Two crystal forms were obtained; the first belongs to the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2 and the second to the hexagonal space group P6(1) or P6(5). The crystals are most likely to contain one omega protein in the asymmetric unit; with V(m) values of 3.2 and 3.5 A(3) Da(-1); respectiv
10666585
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0.030312669, -0.01839361, -0.035610028, 0.003051667, -0.064317435, -0.008360731, 0.002546679, 0.016908744, 0.064692, 0.05310737 ]
Crystallization and preliminary X-ray diffraction studies of Streptococcus pyogenes plasmid pSM19035-encoded omega transcriptional repressor.
ely. The crystals diffract X-rays to 2.4 and 2.9 A resolution for the tetragonal and hexagonal systems; -respectively.
10666585
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Overexpression, purification, crystallization and preliminary structural study of dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD), the fourth enzyme of the dTDP-L-rhamnose synthesis pathway, from Salmonella enterica serovar Typhimurium.
L-Rhamnose is an essential component of the cell wall of many pathogenic bacteria. Its precursor; dTDP-L-rhamnose; is synthesized from alpha-D-glucose-1-phosphate and dTTP via a pathway requiring four distinct enzymes: RmlA; RmlB; RmlC and RmlD. RmlD catalyses the terminal step of this pathway by converting dTDP-6-deoxy-L-lyxo-4-hexulose to dTDP-L-rhamnose. RmlD from -Salmonella enterica serovar Typhimurium has been overexpressed in Escherichia coli. The recombinant protein was purified by a two--step proto
10666586
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-0.06077012, -0.011093489, 0.05277264, -0.003968647, 0.034664646, 0.03988039, -0.0052491794, 0.072325, 0.07205753 ]
Overexpression, purification, crystallization and preliminary structural study of dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD), the fourth enzyme of the dTDP-L-rhamnose synthesis pathway, from Salmonella enterica serovar Typhimurium.
col involving anion-exchange and hydrophobic chromatography. Dynamic light-scattering experiments indicated that the recombinant protein is monodisperse. Crystals of native and selenomethionine-enriched RmlD have been obtained using the sitting-drop vapour-diffusion method with polyethylene glycol as precipitant. Diffraction data have been collected from orthorhombic crystals of both native and selenomethionyl-derivatized protein; allowing tracing of the protein structure.
10666586
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0.007440914, -0.028699718, 0.025986677, 0.021584636, 0.023991795, 0.030694602, -0.00042973107, 0.029949846, 0.021425044 ]
Crystallization and preliminary crystal analysis of yeast hexokinase PI and PII.
Hexokinase is the prime enzyme of the Embden-Meyerhof pathway and is responsible for the first stage of energy conversion. It catalyzes the transfer of a phosphate to glucose to form glucose-6-phosphate. Yeast hexokinase PII is also known to play an important role in glucose signal transduction. Crystals of yeast hexokinase isoforms PI and PII were obtained by vapour-diffusion techniques using the hanging-drop method. Isoform PI crystals belong to the space group P2(1)2(1)2(1); with unit-cell parameters a =
10666587
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-0.012773911, 0.01428222, -0.0053091147, -0.015643703, 0.016564704, -0.056221224, 0.027576696, 0.00034662746, -0.0067273257, 0.0764032, 0.06556473 ]
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Crystallization and preliminary crystal analysis of yeast hexokinase PI and PII.
62.12; b = 78.87; c = 144.74 A. Unit-cell parameters for isoform PII crystals are a = b = 142.81; c = 58.46 A and the space group is I4. Synchrotron diffraction data have been collected to 2.2 A resolution from the isoform PII crystal; whereas isoform PI diffracted to 3.1 A.
10666587
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Crystallization and preliminary X-ray analysis of Thermotoga maritima ribosome recycling factor.
Thermotoga maritima ribosome recycling factor (RRF) is one of the proteins catalyzing the fourth step in prokaryotic protein synthesis; ribosome recycling. The RRF protein was crystallized with ammonium sulfate. Native diffraction data to 2.55 A resolution were obtained at the MAX II synchrotron from a flash-frozen crystal at 100 K. The crystals belong to space group P4(1)2(1)2 or P4(3)2(1)2; with unit-cell parameters a = b = 47; c = 298 A; and probably contain one monomer per asymmetric unit.
10666588
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Crystallization and preliminary X-ray diffraction data for a purple acid phosphatase from sweet potato.
Purple acid phosphatase from sweet potato is a homodimer of 110 kDa. Two forms of the enzyme have been characterized. One contains an Fe-Zn centre similar to that previously reported for red kidney bean purple acid phosphatase. Another isoform; the subject of this work; is the first confirmed example of an Fe-Mn-containing enzyme. Crystals of this protein have been grown from PEG 6000. They have unit-cell parameters a = b = 118.4; c = 287.4 A and have the symmetry of space group P6(5)22; with one dimer per
10666589
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Crystallization and preliminary X-ray diffraction data for a purple acid phosphatase from sweet potato.
asymmetric unit. Diffraction data collected using a conventional X--ray source from a cryocooled crystal extend to 2.90 A resolution. The three-dimensional structure of the enzyme will provide insight into the coordination of this novel binuclear metal centre.
10666589
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-0.006212928, 0.010399179, 0.04164987, -0.03157629, 0.018353054, 0.020838225, 0.02109073, 0.027031219, -0.034818973, 0.07054165, -0.015801435 ]
Crystallization of the N-terminal domain of human sex hormone-binding globulin, the major sex steroid carrier in blood.
The amino-teminal laminin G-like domain of human sex hormone-binding globulin (SHBG); which contains the steroid-binding site and the dimerization domain; has been produced in Escherichia coli; purified to homogeneity and crystallized in complex with 5alpha--dihydrotestosterone (DHT) in two different crystal forms. Native data sets have been collected for tetragonal crystals (space group P4(1)22 or P4(3)22; unit-cell parameters a = 52.2; c = 148.4 A) diffracting to 3.3 A and trigonal crystals (R32; a = 104.
10666590
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Crystallization of the N-terminal domain of human sex hormone-binding globulin, the major sex steroid carrier in blood.
0; c = 84.4 A) diffracting to better than 1.6 A. Since both crystal forms can only accommodate a single monomer in the asymmetric unit and share twofold rotational symmetry; it is proposed that the homodimer of this truncated form of SHBG; as observed in ultracentrifugation experiments; displays C(2) point-group symmetry.
10666590
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0.0077502574, -0.013322425, -0.050296497, 0.07429557, 0.004279345, 0.051071525, -0.064728014, 0.015193176, -0.08413038, -0.078945726, 0.000091345304, -0.10064644, 0.056763954, 0.047356743, -0.032257106, 0.007302613, -0.01861398, -0.00771017, 0.0018757627, 0.0515793, -0.003338958, 0.014244438, 0.011177742, 0.10738115, 0.031615704, -0.057191554, -0.015126364, -0.01807948, 0.06707981, 0.077930175, -0.0062035467, -0.061788257, -0.021339932, 0.061841708, 0.070714414, -0.070714414, 0.027740575, 0.04519202, 0.014591863, -0.048532646, -0.020805432, -0.12304202, -0.040274613, -0.056763954, -0.101608545, -0.049628373, -0.02196797, -0.019936869, 0.03877801, -0.035891708, -0.047463644, 0.052461226, -0.0010021884, 0.006771453, 0.012012899, -0.028969927, -0.050643925, 0.10299825, 0.02525515, -0.01914848, 0.008498558, 0.055213902, -0.017478166, -0.015313439, 0.021941246, 0.012801287, -0.0047570546, 0.058741607, 0.01956272, -0.0032938593, -0.013536225, 0.041236714, -0.27430567, -0.017090654, 0.036185686, 0.02578965, 0.07328002, 0.02728625, -0.009059784, -0.08493213, -0.02611035, -0.020805432, 0.04802487, -0.059062306, -0.09059784, -0.069057465, -0.040969465, 0.037094336, 0.0263776, -0.02441331, -0.03605206, -0.024667198, 0.08359588, -0.00084851956, 0.029157003, -0.0057024523, 0.046608444, -0.040969465, 0.09866879, -0.018547168, -0.0057625836, -0.022542559, 0.02243566, -0.031829506, -0.045218743, -0.11427621, 0.014364701, 0.019469181, -0.066438414, -0.049708545, -0.014190989, -0.0527552, -0.013649806, 0.021607183, -0.044604067, 0.04046169, -0.070874766, -0.06023821, 0.008064277, 0.03471581, -0.026123712, -0.01877433, -0.010656604, 0.019509269, 0.0016018312, 0.024359861, -0.016769953, -0.038537487, -0.04829212, 0.029825129, -0.06312451, 0.032470904, -0.032631256, 0.03174933, 0.06707981, -0.028756127, 0.04372214, -0.012547399, 0.011197786, -0.034154583, -0.040381514, -0.017424716, 0.017919129, 0.024814187, 0.012220018, -0.06542286, 0.016569516, -0.041103087, -0.04674207, 0.009627691, -0.021780895, -0.037308134, -0.044978216, -0.07830432, -0.0041791257, 0.042840216, 0.003701416, -0.08006818, 0.037682287, -0.009066464, 0.015674228, 0.0016820063, 0.040809114, -0.027794026, -0.025843099, 0.019242018, 0.07760947, -0.008378295, -0.24437363, -0.025335323, 0.046982594, 0.053503502, -0.013963826, -0.018426904, 0.044791143, 0.01718419, -0.04487132, 0.06515561, 0.027165988, 0.018360093, 0.01638244, -0.023745185, 0.0266983, 0.026203888, 0.033860605, 0.0255224, 0.0062837214, -0.045272194, 0.041610863, 0.03599861, 0.059489906, -0.01616864, -0.031508803, 0.04487132, 0.010482891, -0.019121755, 0.0070420443, -0.012787924, -0.028702676, -0.10502935, 0.09471349, 0.01781223, -0.01244718, 0.018066118, -0.015406977, 0.03185623, -0.025188336, -0.014885839, -0.029611329, -0.03567791, 0.06707981, -0.0065810373, 0.064781465, -0.02377191, 0.04743692, -0.06927127, -0.033833884, -0.033726983, -0.029985478, -0.012580805, 0.04016771, 0.0018974768, 0.018012667, -0.011712242, 0.013248932, 0.031455353, 0.03009238, 0.013262294, 0.028675953, 0.031241555, -0.048425745, 0.059062306, 0.02323741 ]
[ 0.007970739, -0.0531828, 0.02223522, 0.02430641, 0.00046560005, 0.026310787, 0.014110813, -0.029023377, -0.031027755, 0.0061768214, -0.017357904, -0.056282904, 0.027874202, 0.035170134, 0.012346962, 0.008612139, 0.010609835, 0.049628373, -0.039900463, 0.056870855, -0.026310787, 0.03466236, 0.004660176, 0.054011278, 0.020979146, -0.004402948, -0.0046134074, 0.0126676615, -0.01718419, -0.12881462, -0.069164366, -0.04238589, 0.02371846, 0.03680036, -0.02473401, 0.038484037, -0.035303757, 0.03963321, -0.044123016, 0.044283368, 0.0032721453, 0.0506172, 0.051231872, -0.02339776, 0.02393226, 0.028408702, -0.01697039, -0.054225076, 0.08728393, 0.024172785, 0.07605942, -0.020618357, 0.010516297, 0.043054014, 0.030012203, -0.015139727, 0.011338092, -0.007997463, -0.050403398, -0.01568759, -0.012574124, 0.012373687, -0.12689042, 0.05387765, -0.04888007, -0.0014773929, 0.03685381, 0.029370803, 0.058581255, 0.054038, -0.050029248, 0.045967042, 0.039766837, 0.06601081, 0.04059531, -0.008698996, -0.027139263, -0.058581255, -0.00094539777, -0.06980576, 0.04094274, 0.016048377, 0.03164243, 0.03009238, -0.018974768, -0.035864983, -0.01493929, -0.06718671, -0.03233728, 0.060772706, -0.022515833, 0.0559622, -0.059543356, -0.004212532, 0.004690242, -0.058153655, -0.012440499, 0.012888144, -0.06691946, 0.4261038, -0.033165757, 0.04003409, -0.005041008, 0.029130278, 0.020551544, -0.004777098, -0.026404325, 0.021366658, -0.007215757, -0.007596588, 0.045085117, -0.0031134654, 0.002408593, -0.021607183, -0.0071890317, 0.04930767, 0.05026977, -0.010696691, 0.019616168, 0.010950579, -0.016743228, -0.05558805, 0.076273225, -0.0041924883, 0.013582994, -0.0012101425, -0.021727445, 0.08749773, 0.07413522, -0.003419133, 0.054225076, -0.013449369, 0.03190968, 0.00957424, 0.040274613, -0.053102624, 0.03233728, 0.01920193, 0.032871783, 0.030760504, 0.038858186, -0.028088002, 0.06504871, -0.099844694, -0.048639547, 0.1100002, 0.045031667, 0.04051514, -0.013235569, -0.0065342686, -0.036078785, 0.0077502574, -0.013322425, -0.050296497, 0.07429557, 0.004279345, 0.051071525, -0.064728014, 0.015193176, -0.08413038, -0.078945726, 0.000091345304, -0.10064644, 0.056763954, 0.047356743, -0.032257106, 0.007302613, -0.01861398, -0.00771017, 0.0018757627, 0.0515793, -0.003338958, 0.014244438, 0.011177742, 0.10738115, 0.031615704, -0.057191554, -0.015126364, -0.01807948, 0.06707981, 0.077930175, -0.0062035467, -0.061788257, -0.021339932, 0.061841708, 0.070714414, -0.070714414, 0.027740575, 0.04519202, 0.014591863, -0.048532646, -0.020805432, -0.12304202, -0.040274613, -0.056763954, -0.101608545, -0.049628373, -0.02196797, -0.019936869, 0.03877801, -0.035891708, -0.047463644, 0.052461226, -0.0010021884, 0.006771453, 0.012012899, -0.028969927, -0.050643925, 0.10299825, 0.02525515, -0.01914848, 0.008498558, 0.055213902, -0.017478166, -0.015313439, 0.021941246, 0.012801287, -0.0047570546, 0.058741607, 0.01956272, -0.0032938593, -0.013536225, 0.041236714, -0.27430567, -0.017090654, 0.036185686, 0.02578965, 0.07328002, 0.02728625, -0.009059784, -0.08493213, -0.02611035, -0.020805432, 0.04802487, -0.059062306, -0.09059784, -0.069057465, -0.040969465, 0.037094336, 0.0263776, -0.02441331, -0.03605206, -0.024667198, 0.08359588, -0.00084851956, 0.029157003, -0.0057024523, 0.046608444, -0.040969465, 0.09866879, -0.018547168, -0.0057625836, -0.022542559, 0.02243566, -0.031829506, -0.045218743, -0.11427621, 0.014364701, 0.019469181, -0.066438414, -0.049708545, -0.014190989, -0.0527552, -0.013649806, 0.021607183, -0.044604067, 0.04046169, -0.070874766, -0.06023821, 0.008064277, 0.03471581, -0.026123712, -0.01877433, -0.010656604, 0.019509269, 0.0016018312, 0.024359861, -0.016769953, -0.038537487, -0.04829212, 0.029825129, -0.06312451, 0.032470904, -0.032631256, 0.03174933, 0.06707981, -0.028756127, 0.04372214, -0.012547399, 0.011197786, -0.034154583, -0.040381514, -0.017424716, 0.017919129, 0.024814187, 0.012220018, -0.06542286, 0.016569516, -0.041103087, -0.04674207, 0.009627691, -0.021780895, -0.037308134, -0.044978216, -0.07830432, -0.0041791257, 0.042840216, 0.003701416, -0.08006818, 0.037682287, -0.009066464, 0.015674228, 0.0016820063, 0.040809114, -0.027794026, -0.025843099, 0.019242018, 0.07760947, -0.008378295, -0.24437363, -0.025335323, 0.046982594, 0.053503502, -0.013963826, -0.018426904, 0.044791143, 0.01718419, -0.04487132, 0.06515561, 0.027165988, 0.018360093, 0.01638244, -0.023745185, 0.0266983, 0.026203888, 0.033860605, 0.0255224, 0.0062837214, -0.045272194, 0.041610863, 0.03599861, 0.059489906, -0.01616864, -0.031508803, 0.04487132, 0.010482891, -0.019121755, 0.0070420443, -0.012787924, -0.028702676, -0.10502935, 0.09471349, 0.01781223, -0.01244718, 0.018066118, -0.015406977, 0.03185623, -0.025188336, -0.014885839, -0.029611329, -0.03567791, 0.06707981, -0.0065810373, 0.064781465, -0.02377191, 0.04743692, -0.06927127, -0.033833884, -0.033726983, -0.029985478, -0.012580805, 0.04016771, 0.0018974768, 0.018012667, -0.011712242, 0.013248932, 0.031455353, 0.03009238, 0.013262294, 0.028675953, 0.031241555, -0.048425745, 0.059062306, 0.02323741 ]
The porphobilinogen synthase family of metalloenzymes.
The porphobilinogen synthase (PBGS) family of enzymes catalyzes the first common step in the biosynthesis of the essential tetrapyrroles such as chlorophyll and porphyrin. Although PBGSs are highly conserved at all four levels of protein structure; there is considerable diversity in the use of divalent cations for the catalytically essential and allosteric roles. Assumptions regarding commonalities among the PBGS proteins coupled with the diversity of usage of metal ions has led to a confused literature. Th
10666591
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The porphobilinogen synthase family of metalloenzymes.
e recent publication of crystal structures for three PBGS proteins coupled with more than 50 individual PBGS sequences allows an evaluation of these assumptions. This topical review focuses on the usage of metals by the PBGS family of proteins. It raises doubt concerning a dogma that there has been an evolutionary shift between Zn(II) and Mg(II) at one or more of the divalent metal-binding sites. It also raises the possibility that there may be up to four specific divalent metal ion-binding sites; each serv
10666591
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0.029263236, 0.026433032, 0.038528148, -0.020719225, 0.028622435, -0.05804587, 0.02404338, -0.020545674, -0.06648308, 0.07433289, 0.053827263 ]
The porphobilinogen synthase family of metalloenzymes.
ing a unique function that can be alternatively filled by amino acids in some of the PBGSs.
10666591
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-0.008261726, 0.019995771, 0.024093375, 0.03796935, 0.03919331, -0.093020916, 0.0255435, 0.015179757, -0.052843116, 0.121331625, 0.044727735 ]
Structure of xylose isomerase from Streptomyces diastaticus no. 7 strain M1033 at 1.85 A resolution.
The structure of xylose isomerase (XyI) from Streptomyces diastaticus No. 7 strain M1033 (SDXyI) has been refined at 1.85 A resolution to conventional and free R factors of 0.166 and 0.219; respectively. SDXyI was crystallized in space group P2(1)2(1)2; with unit-cell parameters a = 87.976; b = 98.836; c = 93.927 A. One dimer of the tetrametric molecule is found in each asymmetric unit. Each monomer consists of two domains: a large N-terminal domain (residues 1-320); containing a parallel eight-stranded alp
10666592
[ -0.012822277, 0.01954948, -0.0031157401, 0.016076088, -0.02479284, 0.009961053, 0.012782353, 0.021465836, 0.0032538108, -0.058022965, 0.03720922, -0.053178847, -0.041281477, 0.012769044, 0.037342303, 0.011810867, -0.020188265, 0.00482083, 0.026509574, 0.023621734, -0.03736892, -0.0058488743, -0.016289016, -0.0019429708, 0.012835585, 0.037049524, 0.036570437, 0.0012126933, -0.063718796, -0.14085208, 0.032338485, 0.012416382, 0.012276648, 0.042559046, -0.017579893, -0.056053378, -0.014652129, 0.049851842, -0.0036796674, 0.010546605, 0.04434232, -0.028931635, 0.041494403, -0.018617919, 0.042372733, -0.018777614, -0.07101159, -0.052965917, 0.06536899, -0.043437377, -0.057011556, 0.06962756, -0.006697261, 0.057703573, 0.016142627, 0.0119639095, 0.015929699, -0.013001935, -0.02391451, 0.017366964, 0.051422186, 0.020614121, -0.11828168, 0.026496267, 0.018963927, 0.031752933, 0.0017782841, 0.023794739, 0.05562752, 0.00692017, -0.037182607, -0.031273846, 0.031353693, 0.02230424, 0.0037561886, 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-0.015557075, -0.023808047, -0.056213073, 0.087194145, -0.06957433, 0.063399404, -0.046391755, -0.042000107, 0.11050979, 0.059886087 ]
Structure of xylose isomerase from Streptomyces diastaticus no. 7 strain M1033 at 1.85 A resolution.
ha/beta barrel; and a small C-terminal loop (residues 321-387); containing five helices linked by random coil. The four monomers are essentially identical in the tetramer; possessing non-crystallographic 222 symmetry with one twofold axis essentially coincident with the crystallographic twofold axis in the space group P2(1)2(1)2; which may explain why the diffraction pattern has strong pseudo-I222 symmetry even at medium resolution. The crystal structures of XyIs from different bacterial strains; especially
10666592
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0.041504163, 0.007580181, -0.033630382, -0.070036605, 0.0013245299, 0.04726937, -0.021125752, -0.017816095, 0.018510055, -0.05551682, 0.00043539333, -0.04390633, 0.025836674, -0.024702316, -0.044760436, -0.023554612, -0.043799568, -0.044653673, -0.044787128, -0.02043179, -0.0052947835, -0.24085759, 0.0054015466, -0.0018917089, -0.059040003, -0.05279436, 0.022206727, -0.021846402, -0.04073013, -0.021859748, 0.04153085, -0.06704724, -0.0074200365, 0.07398684, -0.021005644, -0.0029660128, 0.0315485, 0.04807009, -0.013158554, 0.05266091, -0.016134577, 0.021979857, 0.01797624, 0.100410715, -0.07574843, 0.040916964, 0.04073013, 0.021672912, 0.045507777, 0.0068328395, 0.003793427, 0.017896168, 0.005801908, 0.05100608, -0.013292008, 0.045320943, -0.048924197, 0.003996944, 0.03245599, -0.0033413519, 0.03688666, 0.055997256, 0.05717165, -0.057705466, -0.012871629, 0.024328645, -0.01044944, -0.058773097, -0.04430669, -0.02327436, -0.027945247, 0.03459125, -0.004020299, 0.08130011, -0.003930217, 0.039128684, -0.0023187615, -0.0677412, -0.06352405, 0.022099964, -0.021446042, -0.008554394, 0.012004178, -0.05276767, 0.113489196, 0.048603907 ]
Structure of xylose isomerase from Streptomyces diastaticus no. 7 strain M1033 at 1.85 A resolution.
from Streptomyces; are similar. The alpha2 helix of the alpha/beta barrel has a different position in the structures of different XyIs. The conformation of C-terminal fragment 357-364 in the SDXyI structure has a small number of differences to that of other XyIs. Two Co(2+) ions rather than Mg(2+) ions exist in the active site of the SDXyI structure; SDXyI seems to prefer to bind Co(2+) ions rather than Mg(2+) ions.
10666592
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The molecular structure and structural transition of the alpha-helical capsid in filamentous bacteriophage Pf1.
The major coat protein in the capsid of Pf1 filamentous bacteriophage (Inovirus) forms a helical assembly of about 7000 identical protein subunits; each of which contains 46 amino-acid residues and can be closely approximated by a single gently curved alpha-helix. Since the viral DNA occupies the core of the tubular capsid and appears to make no significant specific interactions with the capsid proteins; the capsid is a simple model system for the study of the static and dynamic properties of alpha-helix as
10666593
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The molecular structure and structural transition of the alpha-helical capsid in filamentous bacteriophage Pf1.
sembly. The capsid undergoes a reversible temperature-induced structural transition at about 283 K between two slightly different helix forms. The two forms can coexist without an intermediate state; consistent with a first-order structural phase transition. The molecular model of the higher temperature form was refined using improved X-ray fibre diffraction data and new refinement and validation methods. The refinement indicates that the two forms are related by a change in the orientation of the capsid su
10666593
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-0.068380736, 0.007833066, -0.014918219, 0.076073565, 0.02063442, 0.059726298, 0.014771307, 0.049389053, 0.033736277, -0.055131968, 0.13206029, 0.00004502302 ]
The molecular structure and structural transition of the alpha-helical capsid in filamentous bacteriophage Pf1.
bunits within the virion; without a significant change in local conformation of the subunits. On the higher temperature diffraction pattern there is a region of observed intensity that is not consistent with a simple helix of identical subunits; it is proposed that the structure involves groups of three subunits which each have a slightly different orientation within the group. The grouping of subunits suggests that a change in subunit libration frequency could be the basis of the Pf1 structural transition;
10666593
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0.017202722, 0.011350318, -0.05275858, -0.036358472, 0.017109083, -0.02224582, 0.027021382, -0.033228274, -0.039729457, 0.109102175, 0.09775855 ]
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0.017202722, 0.011350318, -0.05275858, -0.036358472, 0.017109083, -0.02224582, 0.027021382, -0.033228274, -0.039729457, 0.109102175, 0.09775855 ]
The molecular structure and structural transition of the alpha-helical capsid in filamentous bacteriophage Pf1.
calculations from the model are used to explore this idea.
10666593
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-0.01442664, -0.03409691, -0.022797817, 0.0057560164, 0.0049541667, -0.044690643, -0.031089144, -0.012476915, 0.12840243, 0.06835353 ]
Towards the charge-density study of proteins: a room-temperature scorpion-toxin structure at 0.96 A resolution as a first test case.
The number of protein structures refined at a resolution higher than 1.0 A is continuously increasing. Subatomic structures may deserve a more sophisticated model than the spherical atomic electron density. In very high resolution structural studies (d < 0.5 A) of small peptides; a multipolar atom model is used to describe the valence electron density. This allows a much more accurate determination of the anisotropic thermal displacement parameters and the estimate of atomic charges. This information is of
10666594
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Towards the charge-density study of proteins: a room-temperature scorpion-toxin structure at 0.96 A resolution as a first test case.
paramount importance in the understanding of biological processes involving enzymes and metalloproteins. The structure of the scorpion Androctonus australis Hector toxin II has been refined at 0.96 A resolution using synchrotron diffraction data collected at room temperature. Refinement with a multipolar electron-density model in which the multipole populations are transferred from previous peptide studies led to the observation of valence electrons on covalent bonds of the most ordered residues. The refine
10666594
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Towards the charge-density study of proteins: a room-temperature scorpion-toxin structure at 0.96 A resolution as a first test case.
d net charges of the peptide-bond atoms were of the correct sign but were underestimated. Such protein-structure refinements against higher resolution data collected at cryogenic temperature will enable the calculation of experimental atomic charges and properties such as electrostatic potentials.
10666594
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Mass-spectrometry assisted heavy-atom derivative screening of human Fc gamma RIII crystals.
A heavy-atom screening method aided by mass spectrometry is described here. Using mass spectrometry; several heavy-atom compounds have been screened in order to obtain potential phasing derivatives for the crystals of a human immunoglobulin Fc receptor; Fc gamma RIII. Of these; HgCl(2); trimethyllead acetate (TMLA); KAu(CN)(2); K(2)PtCl(4) and PbAc(2) reacted with Fc gamma RIII in solution; whereas KAuCl(4); ethylmercuric thiosalicylate (EMTS) and Na(2)WO(4) did not. To validate the mass-spectrometry result
10666595
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