Refinement of protein structures using a combination of quantum-mechanical calculations with neutron and X-ray crystallographic data
A method has been developed to combine quantum-mechanical calculations with joint crystallographic refinement against X-ray and neutron data. Applications to structures of the galectin-3C–lactose complex and lytic polysaccharide monooxygenase show that it can improve the geometry of hydrogen bonds, particularly those involving water molecules, as well as determine the protonation states of key residues.