嗜热栖热菌surE蛋白的结晶及初步X射线晶体学分析
Crystallization and preliminary X-ray crystallographic analysis of the surE protein from Thermotoga maritima.
作者信息
Kwak J E, Ha K S, Lee J Y, Im Y J, Park S H, Eom S H, Suh S W
机构信息
School of Chemistry and Molecular Engineering, Seoul National University, Seoul 151-742, South Korea.
出版信息
Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):612-3. doi: 10.1107/s0907444901002141.
The surE protein from Thermotoga maritima is a 247-residue protein of unknown function. Its homologues are well conserved among both the eubacteria and the archaea. It has been overexpressed in soluble form in Escherichia coli. The protein has been crystallized at 296 K using 2-propanol as a precipitant. X-ray diffraction data have been collected to 1.9 A resolution using synchrotron radiation. The crystals belong to the trigonal space group P3(1)21 (or P3(2)21), with unit-cell parameters a = b = 115.96, c = 78.60 A, alpha = beta = 90, gamma = 120 degrees. The asymmetric unit contains two monomers of the surE protein, with a corresponding V(M) of 2.72 A(3) Da(-1) and a solvent content of 54.7%.
来自嗜热栖热菌的surE蛋白是一种由247个氨基酸残基组成、功能未知的蛋白质。其同源物在真细菌和古细菌中都高度保守。它已在大肠杆菌中以可溶形式过量表达。该蛋白使用2-丙醇作为沉淀剂在296 K下结晶。利用同步辐射收集了分辨率为1.9 Å的X射线衍射数据。晶体属于三方晶系空间群P3(1)21（或P3(2)21），晶胞参数a = b = 115.96，c = 78.60 Å，α = β = 90°，γ = 120°。不对称单元包含两个surE蛋白单体，相应的V(M)为2.72 ų Da⁻¹，溶剂含量为54.7%。
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