Refinement of protein structures using a combination of quantum-mechanical calculations with neutron and X-ray crystallographic data.

ABSTRACT: Neutron crystallography is a powerful method to determine the positions of H atoms in macromolecular structures. However, it is sometimes hard to judge what would constitute a chemically reasonable model, and the geometry of H atoms depends more on the surroundings (for example the formation of hydrogen bonds) than heavy atoms, so that the empirical geometry information for the H atoms used to supplement the experimental data is often less accurate. These problems may be reduced by using quantum-mechanical calculations. A method has therefore been developed to combine quantum-mechanical calculations with joint crystallographic refinement against X-ray and neutron data. A first validation of this method is provided by re-refining the structure of the galectin-3 carbohydrate-recognition doma

SUBMITTER: Caldararu O 

PROVIDER: S-EPMC6465982 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature