Packing interface energetics in different crystal forms of the λ Cro dimer.

ABSTRACT: Variation among crystal structures of the λ Cro dimer highlights conformational flexibility. The structures range from a wild type closed to a mutant fully open conformation, but it is unclear if each represents a stable solution state or if one may be the result of crystal packing. Here we use molecular dynamics (MD) simulation to investigate the energetics of crystal packing interfaces and the influence of site-directed mutagenesis on them in order to examine the effect of crystal packing on wild type and mutant Cro dimer conformation. Replica exchange MD of mutant Cro in solution shows that the observed conformational differences between the wild type and mutant protein are not the direct consequence of mutation. Instead, simulation of Cro in different crystal environments reveals that

SUBMITTER: Ahlstrom LS 

PROVIDER: S-EPMC4018431 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature