百日咳博德特氏菌自转运蛋白百日咳毒素跨膜结构域P30的结晶及初步X射线衍射分析
Crystallization and preliminary X-ray diffraction analysis of P30, the transmembrane domain of pertactin, an autotransporter from Bordetella pertussis.
作者信息
Zhu Yanshi, Black Isobel, Roszak Aleksander W, Isaacs Neil W
机构信息
Department of Chemistry and WestChem, Glasgow Biomedical Research Centre, University of Glasgow, 120 University Place, Glasgow G12 8TA, Scotland.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jul 1;63(Pt 7):593-5. doi: 10.1107/S1744309107028308. Epub 2007 Jun 15.
P30, the 32 kDa transmembrane C-terminal domain of pertactin from Bordetella pertussis, is supposed to form a beta-barrel inserted into the outer membrane for the translocation of the passenger domain. P30 was cloned and expressed in inclusion bodies in Escherichia coli. After refolding and purification, the protein was crystallized using the sitting-drop vapour-diffusion method at 292 K. The crystals diffract to a resolution limit of 3.5 A using synchrotron radiation and belong to the hexagonal space group P6(1)22, with unit-cell parameters a = b = 123.27, c = 134.43 A.
P30是百日咳博德特氏菌丝状血凝素的32 kDa跨膜C末端结构域，被认为可形成插入外膜的β桶，用于转运乘客结构域。P30在大肠杆菌中克隆并在包涵体中表达。经重折叠和纯化后，采用坐滴气相扩散法于292 K使该蛋白结晶。利用同步辐射，晶体衍射分辨率极限为3.5 Å，属于六方空间群P6(1)22，晶胞参数a = b = 123.27，c = 134.43 Å。
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