Achour A, Harris R A, Persson K, Sundbäck J, Sentman C L, Schneider G, Lindqvist Y, Kärre K
Microbiology and Tumorbiology Center, Karolinska Institutet, Stockholm, Sweden.
Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):260-2. doi: 10.1107/S0907444998005265. Epub 1999 Jan 1.
A truncated soluble form of the murine class I major histocompatibility antigen complex H-2Dd was cloned using an Escherichia coli based system. It was expressed, refolded in vitro and crystallized in a complex with murine beta2 microglobulin and the peptide RGPGRAFVTI from the V3-loop of the gp160 HIV-1 protein. Crystals belonging to the space group P212121 with cell dimensions a = 51.3, b = 92.5, c = 108.8 A were obtained using two different crystallization conditions. The crystals contain one complex per asymmetric unit and diffract to at least 2.4 A resolution.
利用基于大肠杆菌的系统克隆了小鼠I类主要组织相容性抗原复合物H-2Dd的截短可溶性形式。它在体外表达、重折叠，并与小鼠β2微球蛋白以及来自gp160 HIV-1蛋白V3环的肽RGPGRAFVTI形成复合物后结晶。使用两种不同的结晶条件获得了属于空间群P212121的晶体，其晶胞参数为a = 51.3、b = 92.5、c = 108.8 Å。每个不对称单元的晶体包含一个复合物，并且衍射分辨率至少为2.4 Å。
