X-ray refinement significantly underestimates the level of microscopic heterogeneity in biomolecular crystals.

ABSTRACT: Biomolecular X-ray structures typically provide a static, time- and ensemble-averaged view of molecular ensembles in crystals. In the absence of rigid-body motions and lattice defects, B-factors are thought to accurately reflect the structural heterogeneity of such ensembles. In order to study the effects of averaging on B-factors, we employ molecular dynamics simulations to controllably manipulate microscopic heterogeneity of a crystal containing 216 copies of villin headpiece. Using average structure factors derived from simulation, we analyse how well this heterogeneity is captured by high-resolution molecular-replacement-based model refinement. We find that both isotropic and anisotropic refined B-factors often significantly deviate from their actual values known from simulation: even

SUBMITTER: Kuzmanic A 

PROVIDER: S-EPMC3926004 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature