Open AccessCrystallization and preliminary X‐ray analysis of bacteriophage T4 UvsY recombination mediator protein
Author(s) -
Xu Hang,
Rould Mark A.,
Beernink Hans T. H.,
Morrical Scott W.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106036074
Subject(s) - bacteriophage , crystallization , recombination , materials science , crystallography , chemistry , biophysics , biology , biochemistry , escherichia coli , gene , organic chemistry
Bacteriophage T4 UvsY protein is considered to be the prototype of recombination mediator proteins, a class of proteins which assist in the loading of recombinases onto DNA. Wild‐type and Se‐substituted UvsY protein have been expressed and purified and crystallized by hanging‐drop vapor diffusion. The crystals diffract to 2.4 Å using in‐house facilities and to 2.2 Å at NSLS, Brookhaven National Laboratory. The crystals belong to space group P 422, P 4 2 22, P 42 1 2 or P 4 2 2 1 2, the ambiguity arising from pseudo‐centering, with unit‐cell parameters a = b = 76.93, c = 269.8 Å. Previous biophysical characterization of UvsY indicates that it exists primarily as a hexamer in solution. Along with the absence of a crystallographic threefold, this suggests that the asymmetric unit of these crystals is likely to contain either three monomers, giving a solvent content of 71%, or six monomers, giving a solvent content of 41%.