Crystallization and preliminary crystallographic analysis of recombinant immunoglobulin G-binding protein from Streptococcus suis.
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 P2(1)2(1)2(1), with unit-cell parameters a = 38.98, b = 43.94, c = 78.17 A and one molecule in the asymmetric unit. Diffraction data were collected to 2.60 A resolution.
Khan
Abdul Hamid
AH
Center for Molecular Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
Chu
Fuliang
F
Feng
Youjun
Y
Zhang
Qinagmin
Q
Qi
Jianxun
J
Gao
George Fu
GF
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D017011:Streptococcus suis / Q000737:chemistry*
D001426:Bacterial Proteins; C034284:IgG Fc-binding protein, Streptococcus; D011994:Recombinant Proteins