
Crystallization and preliminary crystallographic analysis of recombinant immunoglobulin G‐binding protein from Streptococcus suis
Author(s) -
Khan Abdul Hamid,
Chu Fuliang,
Feng Youjun,
Zhang Qinagmin,
Qi Jianxun,
Gao George Fu
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108020149
Subject(s) - recombinant dna , streptococcus suis , escherichia coli , crystallization , antibody , chemistry , resolution (logic) , protein g , crystallography , microbiology and biotechnology , biology , biochemistry , immunology , gene , virulence , computer science , organic chemistry , artificial intelligence
Streptococcus suis , an important zoonotic pathogen, expresses immunoglobulin G‐binding protein, which is thought to be helpful to the organism in eluding the host defence system. Recombinant IgG‐binding protein expressed in Escherichia coli has been crystallized using the hanging‐drop vapour‐diffusion method. The crystals belonged to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 38.98, b = 43.94, c = 78.17 Å and one molecule in the asymmetric unit. Diffraction data were collected to 2.60 Å resolution.