Ensemble refinement of protein crystal structures: validation and application.

ABSTRACT: X-ray crystallography typically uses a single set of coordinates and B factors to describe macromolecular conformations. Refinement of multiple copies of the entire structure has been previously used in specific cases as an alternative means of representing structural flexibility. Here, we systematically validate this method by using simulated diffraction data, and we find that ensemble refinement produces better representations of the distributions of atomic positions in the simulated structures than single-conformer refinements. Comparison of principal components calculated from the refined ensembles and simulations shows that concerted motions are captured locally, but that correlations dissipate over long distances. Ensemble refinement is also used on 50 experimental structures of vary

SUBMITTER: Levin EJ 

PROVIDER: S-EPMC2039884 | biostudies-literature | 2007 Sep

REPOSITORIES: biostudies-literature