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来自大肠杆菌的天冬氨酸转氨酶突变体的结晶及初步X射线研究。

Crystallization and preliminary X-ray studies of an aspartate aminotransferase mutant from Escherichia coli.

作者信息

Jäger J, Köhler E, Tucker P, Sauder U, Housley-Markovic Z, Fotheringham I, Edwards M, Hunter M, Kirschner K, Jansonius J N

机构信息

Department of Structural Biology, University of Basel, Switzerland.

出版信息

J Mol Biol. 1989 Oct 5;209(3):499-501. doi: 10.1016/0022-2836(89)90014-4.

DOI:10.1016/0022-2836(89)90014-4
PMID:2685322
Abstract

Mutant aspartate aminotransferase V39L (Val39 replaced by Leu) from Escherichia coli has been crystallized into a monoclinic cell from a polyethylene glycol solution (pH 7.5) by vapor diffusion. The space group and the unit cell dimensions have been determined using a precession camera, a CAD4 diffractometer and a Nicolet Xentronics area detector to be P2(1) with a = 86.8 A, b = 79.9 A, c = 89.4 A, beta = 118.74 degrees. The crystals diffract to better than 2.3 A and are suitable for X-ray structure analysis.

摘要

来自大肠杆菌的突变天冬氨酸转氨酶V39L(缬氨酸39被亮氨酸取代)已通过气相扩散法,从聚乙二醇溶液(pH 7.5)中结晶到单斜晶胞中。使用进动相机、CAD4衍射仪和Nicolet Xentronics面探测器确定其空间群和晶胞尺寸为P2(1),a = 86.8 Å,b = 79.9 Å,c = 89.4 Å,β = 118.74°。这些晶体的衍射分辨率优于2.3 Å,适合进行X射线结构分析。

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