Expression, purification, crystallization and preliminary X-ray diffraction analysis of grass carp beta2-microglobulin.
Beta(2)-microglobulin (beta(2)m) is an essential subunit of MHC I molecules; it stabilizes the structure of MHC I and plays a pivotal role in coreceptor recognition. To date, structures of beta(2)m have been solved for three different mammals: human, mouse and cattle. In order to illuminate the molecular evolutionary origin of beta2m, an understanding of its structure in lower vertebrates becomes important. Here, grass carp (Ctenopharyngodon idellus) beta(2)m (Ctid-beta(2)m) was expressed, purified and crystallized. Diffraction data were collected to a resolution of 2.5 A. The crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 38.72, b = 40.65, c = 71.12 A. The Matthews coefficient and the solvent content were calculated to be 2.56 A Da(-1) and 52.07%, respectively, for one molecule per asymmetric unit. The structure has been solved by molecular replacement using monomeric human beta(2)m as a model.
Chen
Weihong
W
Department of Microbiology and Immunology, College of Veterinary Medicine, China Agricultural University, Beijing 100094, People's Republic of China.
Chu
Fuliang
F
Peng
Hao
H
Zhang
Jianhua
J
Qi
Jianxun
J
Jiang
Fan
F
Xia
Chun
C
Gao
Feng
F
D000818:Animals; D002347:Carps / Q000235:genetics / Q000378:metabolism*; D002850:Chromatography, Gel; D003460:Crystallization; D015870:Gene Expression; D014961:X-Ray Diffraction; D001613:beta 2-Microglobulin / Q000097:blood* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*
D001613:beta 2-Microglobulin