大肠杆菌应激蛋白YciE的表达、结晶及初步晶体学分析
Expression, crystallization and preliminary crystallographic analysis of YciE, a stress protein from Escherichia coli.
作者信息
Liu Deqian, Zhao Yonghong, Fan Xiuzhen, Sun Yuan, Fox Robert O
机构信息
The Department of Human Biological Chemistry and Genetics, The University of Texas Medical Branch, Galveston, TX 77555-0647, USA.
出版信息
Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1888-9. doi: 10.1107/S0907444904018591. Epub 2004 Sep 23.
The stress protein Escherichia coli YciE was overexpressed and purified in three chromatographic steps. Crystals were obtained using PEG 4000 as a precipitant. The YciE protein crystals diffracted to 3.0 A resolution using a rotating-anode X-ray source. The lattice type is rhombohedral, with unit-cell parameters a = b = 64.2, c = 167.9 A, alpha = beta = 90, gamma = 120 degrees. The crystal belongs to space group R32.
应激蛋白大肠杆菌YciE通过三步色谱法进行过表达和纯化。使用聚乙二醇4000作为沉淀剂获得晶体。利用旋转阳极X射线源，YciE蛋白晶体的衍射分辨率达到3.0埃。晶格类型为菱面体，晶胞参数a = b = 64.2，c = 167.9埃，α = β = 90°，γ = 120°。该晶体属于空间群R32。
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