Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 64, Part 3 (March 2008)

crystallization communications

 

Expression, purification, crystallization and preliminary X-ray diffraction analysis of grass carp ₂-microglobulin

W. Chen, F. Chu, H. Peng, J. Zhang, J. Qi, F. Jiang, C. Xia and F. Gao

Abstract: ₂-Microglobulin (₂m) 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 ₂m have been solved for three different mammals: human, mouse and cattle. In order to illuminate the molecular evolutionary origin of 2m, an understanding of its structure in lower vertebrates becomes important. Here, grass carp (Ctenopharyngodon idellus) ₂m (Ctid-₂m) was expressed, purified and crystallized. Diffraction data were collected to a resolution of 2.5 Å. The crystal belongs to space group P2₁2₁2₁, with unit-cell parameters a = 38.72, b = 40.65, c = 71.12 Å. The Matthews coefficient and the solvent content were calculated to be 2.56 Å Da^-1 and 52.07%, respectively, for one molecule per asymmetric unit. The structure has been solved by molecular replacement using monomeric human ₂m as a model.

Keywords: ₂-microglobulin; MHC I.

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