Souchon H, Spinelli S, Béguin P, Alzari P M
Unité d'Immunologie Structurale, URA 359 CNRS, Institut Pasteur, Paris, France.
J Mol Biol. 1994 Jan 28;235(4):1348-50. doi: 10.1006/jmbi.1994.1089.
The catalytic domain of a thermostable xylanase from Clostridium thermocellum has been expressed in Escherichia coli and crystallized from a polyethylene glycol 2000 solution by the hanging drop method. Crystals belong to the triclinic space group P1 with cell dimensions a = 46.8 A, b = 50.8 A, c = 70.3 A, alpha = 100.7 degrees, beta = 83.8 degrees, gamma = 101.6 degrees, and two molecules in the unit cell. These crystals diffract X-rays to at least 1.8 A resolution and are suitable for high-resolution X-ray analysis.
来自热纤梭菌的一种耐热木聚糖酶的催化结构域已在大肠杆菌中表达,并通过悬滴法从聚乙二醇2000溶液中结晶。晶体属于三斜晶系空间群P1,晶胞参数为a = 46.8 Å,b = 50.8 Å,c = 70.3 Å,α = 100.7°,β = 83.8°,γ = 101.6°,晶胞中有两个分子。这些晶体的X射线衍射分辨率至少为1.8 Å,适合进行高分辨率X射线分析。