DsbA（一种大肠杆菌蛋白，在体内二硫键形成过程中发挥作用）的结晶。
Crystallization of DsbA, an Escherichia coli protein required for disulphide bond formation in vivo.
作者信息
Martin J L, Waksman G, Bardwell J C, Beckwith J, Kuriyan J
机构信息
Howard Hughes Medical Institute, Rockefeller University, New York, NY 10021.
出版信息
J Mol Biol. 1993 Apr 5;230(3):1097-100. doi: 10.1006/jmbi.1993.1226.
DsbA is a 21 kDa protein that facilitates disulphide bond formation and is required for the correct folding and stability of a number of exported proteins in Escherichia coli. Crystals of oxidized DsbA have been obtained from polyethylene glycol 8000 (20 to 25%), 0.1 M-cacodylate buffer (pH 6.5) and 1% 2-methyl-2,4-pentanediol. Oxidation of the protein is critical for reproducibly obtaining high quality crystals. The resulting crystals diffract to 2 A and belong to the monoclinic space group C2 with cell dimensions a = 117.5 A, b = 65.0 A, c76.3 A, beta = 126.3 degrees with two molecules in the asymmetric unit.
二硫键异构酶A（DsbA）是一种21 kDa的蛋白质，它促进二硫键的形成，是大肠杆菌中许多输出蛋白正确折叠和稳定所必需的。已从含20%至25%聚乙二醇8000、0.1 M二甲胂酸盐缓冲液（pH 6.5）和1% 2-甲基-2,4-戊二醇中获得氧化型二硫键异构酶A的晶体。蛋白质的氧化对于可重复地获得高质量晶体至关重要。所得晶体的衍射分辨率为2 Å，属于单斜空间群C2，晶胞参数为a = 117.5 Å，b = 65.0 Å，c = 76.3 Å，β = 126.3°，不对称单位中有两个分子。
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