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来自大肠杆菌K12的钙激活磷酸烯醇式丙酮酸羧激酶的结晶。

Crystallization of the calcium-activated phosphoenolpyruvate carboxykinase from Escherichia coli K12.

作者信息

Delbaere L T, Vandonselaar M, Glaeske D, Jabs C, Goldie H

机构信息

Department of Biochemistry, University of Saskatchewan, Saskatoon, Canada.

出版信息

J Mol Biol. 1991 Jun 20;219(4):593-4. doi: 10.1016/0022-2836(91)90654-o.

Abstract

Single crystals of phosphoenolpyruvate carboxykinase from Escherichia coli K12 have been grown in the orthorhombic crystal system. Single crystals developed to a maximum size of 0.25 mm x 0.25 mm x 1.5 mm by the technique of washing and reseeding. The space group is P2(1)2(1)2(1), with a = 77.24 A, b = 89.18 A, c = 93.24 A and Z = 4; there is one enzyme molecule per crystallographic asymmetric unit and the solvent content is estimated to be 59%. The crystals diffract to at least 2.8 A d spacings and decompose in the X-ray beam after approximately two days of exposure.

摘要

已通过洗涤和再接种技术在正交晶系中培养出大肠杆菌K12磷酸烯醇丙酮酸羧激酶的单晶。单晶通过该技术生长至最大尺寸为0.25毫米×0.25毫米×1.5毫米。空间群为P2(1)2(1)2(1),a = 77.24埃,b = 89.18埃,c = 93.24埃,Z = 4;每个晶体学不对称单元中有一个酶分子,溶剂含量估计为59%。这些晶体在至少2.8埃的d间距处发生衍射,并在暴露约两天后在X射线束中分解。

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