Homology-based hydrogen bond information improves crystallographic structures in the PDB.

ABSTRACT: The Protein Data Bank (PDB) is the global archive for structural information on macromolecules, and a popular resource for researchers, teachers, and students, amassing more than one million unique users each year. Crystallographic structure models in the PDB (more than 100,000 entries) are optimized against the crystal diffraction data and geometrical restraints. This process of crystallographic refinement typically ignored hydrogen bond (H-bond) distances as a source of information. However, H-bond restraints can improve structures at low resolution where diffraction data are limited. To improve low-resolution structure refinement, we present methods for deriving H-bond information either globally from well-refined high-resolution structures from the PDB-REDO databank, or specifically fr

SUBMITTER: van Beusekom B 

PROVIDER: S-EPMC5818736 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature