Dynamics may significantly influence the estimation of interatomic distances in biomolecular X-ray structures.

ABSTRACT: Atomic positions obtained by X-ray crystallography are time and space averages over many molecules in the crystal. Importantly, interatomic distances, calculated between such average positions and frequently used in structural and mechanistic analyses, can be substantially different from the more appropriate time-average and ensemble-average interatomic distances. Using crystallographic B-factors, one can deduce corrections, which have so far been applied exclusively to small molecules, to obtain correct average distances as a function of the type of atomic motion. Here, using 4774 high-quality protein X-ray structures, we study the significance of such corrections for different types of atomic motion. Importantly, we show that for distances shorter than 5 Å, corrections greater than 0.5 Å

SUBMITTER: Kuzmanic A 

PROVIDER: S-EPMC3171141 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature