Summarize these texts into a summary:

We recorded one-dimensional (1D) traces of
individual kinesin dimers labeled with a single
fluorophore (degree of labeling of 1, DOL1) on
the stalk walking along the microtubule axis
(on-axis displacement) with a temporal reso-
lution of ~1 ms and a precision of s ≈ 1.7 nm
(NAME_1. 2, B and C). These initial measurements
were performed at a 10 mM ATP concentration,
providing a walking speed of ~280 nm/s. The
traces were recorded with run lengths up to
~180 nm. On the basis of the residual noise
and the number of localizations between steps,
we determined a median precision of the mea-
sured step size of 0.57 nm (NAME_1. 2D). A histo-
gram of all kinesin center-of-mass steps revealed
a size range of ~3 to 11 nm (NAME_1. 2E), with
equally high peaks centered at 8 and 4 nm,
corresponding to expected regular steps and
substeps, respectively. The latter have so far
not been observed without attaching a much
bigger bead to the protein (27).