Multistart simulated annealing refinement of the crystal structure of the 70S ribosome.

ABSTRACT: A macromolecular X-ray crystal structure is usually represented as a single static model with a single set of temperature factors representing a simple approximation of motion and disorder of the structure. Multiconformer representations of small proteins have been shown to better describe anisotropic motion and disorder and improve the quality of their electron density maps. Here, we apply multistart simulated annealing crystallographic refinement to a 70S ribosome-RF1 translation termination complex that was recently solved at 3.2 A resolution. The analysis improves the interpretability of the electron density map of this 2.5-MDa ribonucleoprotein complex and provides insights into its structural dynamics. We also used multistart refinement and conventional Fourier difference maps to add

SUBMITTER: Korostelev A 

PROVIDER: S-EPMC2775320 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature