Open AccessCloning, expression, purification, crystallization and preliminary X‐ray diffraction analysis of the collagen‐binding region of RspB from Erysipelothrix rhusiopathiae
Author(s) -
Devi Aribam Swarmistha,
Ogawa Yohsuke,
Shimoji Yoshihiro,
Ponnuraj Karthe
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109035581
Subject(s) - erysipelothrix rhusiopathiae , crystallization , resolution (logic) , monoclinic crystal system , crystallography , chemistry , escherichia coli , derivative (finance) , diffraction , microbiology and biotechnology , materials science , biology , biochemistry , optics , crystal structure , physics , organic chemistry , artificial intelligence , computer science , gene , financial economics , economics
RspB is a surface adhesin of Erysipelothrix rhusiopathiae . A recombinant form of the collagen‐binding region of this protein, RspB (31–348) , has been overexpressed in Escherichia coli in native and selenomethionine‐derivative forms and purified using affinity and gel‐permeation chromatography. Thin plate‐like crystals were obtained by the hanging‐drop vapour‐diffusion method using the same condition for both forms. The native crystals diffracted to a resolution of 2.5 Å using an in‐house X‐ray source, while the selenomethionine‐derivative crystals diffracted to a resolution of 2.2 Å using synchrotron radiation. The crystals belonged to the monoclinic space group P 2 1 , with unit‐cell parameters a = 46.19, b = 66.65, c = 101.72 Å, β = 94.11°.