一种古生菌型磷酸烯醇式丙酮酸羧化酶的表达、纯化及结晶
Expression, purification and crystallization of an archaeal-type phosphoenolpyruvate carboxylase.
作者信息
Dharmarajan Lakshmi, Kraszewski Jessica L, Mukhopadhyay Biswarup, Dunten Pete W
机构信息
Virginia Bioinformatics Institute, USA.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Nov 1;65(Pt 11):1193-6. doi: 10.1107/S1744309109042663. Epub 2009 Oct 30.
Abstract
An archaeal-type phosphoenolpyruvate carboxylase (PepcA) from Clostridium perfringens has been expressed in Escherichia coli in a soluble form with an amino-terminal His tag. The recombinant protein is enzymatically active and two crystal forms have been obtained. Complete diffraction data extending to 3.13 angstrom resolution have been measured from a crystal soaked in KAu(CN)(2), using radiation at a wavelength just above the Au L(III) edge. The asymmetric unit contains two tetramers of PepcA.
摘要
产气荚膜梭菌的一种古菌型磷酸烯醇式丙酮酸羧化酶（PepcA）已在大肠杆菌中以带有氨基末端His标签的可溶形式表达。重组蛋白具有酶活性，并获得了两种晶体形式。使用波长略高于金L(III) 边的辐射，从浸泡在KAu(CN)₂中的晶体测量了分辨率达3.13埃的完整衍射数据。不对称单元包含两个PepcA四聚体。
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