伤寒沙门氏菌PilS的结晶及初步X射线衍射分析
Crystallization and preliminary X-ray diffraction analysis of Salmonella typhi PilS.
作者信息
Balakrishna Asha M, Tan Yvonne Yih-Wan, Mok Henry Yu-Keung, Saxena Anand M, Swaminathan Kunchithapadam
机构信息
Department of Biological Sciences, National University of Singapore, Singapore 117543, Singapore.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt 10):1024-6. doi: 10.1107/S174430910603661X. Epub 2006 Sep 30.
Abstract
The structure determination of PilS, a type IV pilin, by X-ray crystallography is reported. The recombinant protein from Salmonella typhi was overexpressed, purified and crystallized. The crystals belong to space group P2(1)2(1)2, with unit-cell parameters a = 77.88, b = 114.53, c = 31.75 A. The selenomethionine derivative of the PilS protein was overexpressed, purified and crystallized in the same space group. Data sets have been collected to 2.1 A resolution from the selenomethionine-derivative crystal using synchrotron radiation for multiwavelength anomalous dispersion (MAD) phasing.
摘要
报道了通过X射线晶体学对IV型菌毛蛋白PilS的结构测定。伤寒沙门氏菌的重组蛋白被过量表达、纯化并结晶。晶体属于空间群P2(1)2(1)2，晶胞参数a = 77.88，b = 114.53，c = 31.75 Å。PilS蛋白的硒代甲硫氨酸衍生物在相同空间群中被过量表达、纯化并结晶。使用同步辐射进行多波长反常散射（MAD）相位分析，已从硒代甲硫氨酸衍生物晶体收集到分辨率为2.1 Å的数据集。
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