High-resolution structure prediction and the crystallographic phase problem.

ABSTRACT: The energy-based refinement of low-resolution protein structure models to atomic-level accuracy is a major challenge for computational structural biology. Here we describe a new approach to refining protein structure models that focuses sampling in regions most likely to contain errors while allowing the whole structure to relax in a physically realistic all-atom force field. In applications to models produced using nuclear magnetic resonance data and to comparative models based on distant structural homologues, the method can significantly improve the accuracy of the structures in terms of both the backbone conformations and the placement of core side chains. Furthermore, the resulting models satisfy a particularly stringent test: they provide significantly better solutions to the X-ray c

SUBMITTER: Qian B 

PROVIDER: S-EPMC2504711 | biostudies-literature | 2007 Nov

REPOSITORIES: biostudies-literature