来自大肠杆菌的β-羟基癸酰硫酯脱水酶的结晶及初步X射线分析。

Crystallization and preliminary X-ray analysis of beta-hydroxydecanoyl thiol ester dehydrase from Escherichia coli.

作者信息

Sharma A, Henderson B S, Schwab J M, Smith J L

机构信息

Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907.

出版信息

J Biol Chem. 1990 Mar 25;265(9):5110-2.

PMID:2180957

Abstract

Escherichia coli beta-hydroxydecanoyl thiol ester dehydrase, a key enzyme for the biosynthesis of unsaturated fatty acids in E. coli, has been crystallized by the vapor diffusion method at pH 5.0-5.5 using 20% (w/v) polyethylene glycol (molecular weight 8000) as a precipitant. Two crystal forms have been characterized, and both diffract to at least 1.6 A. The orthorhombic crystals belong to space group P2(1)2(1)2(1), with cell constants of a = 68.4 A, b = 87.3 A, and c = 60.3 A. Monoclinic crystals are of space group C2, with a = 131.9 A, b = 71.5 A, c = 92.5 A, and beta = 103.5 degrees.

摘要

大肠杆菌β-羟基癸酰硫酯脱水酶是大肠杆菌中不饱和脂肪酸生物合成的关键酶，已通过气相扩散法在pH 5.0 - 5.5条件下，使用20%（w/v）聚乙二醇（分子量8000）作为沉淀剂进行了结晶。已鉴定出两种晶体形式，且两者的衍射分辨率至少达到1.6 Å。正交晶体属于空间群P2(1)2(1)2(1)，晶胞参数为a = 68.4 Å，b = 87.3 Å，c = 60.3 Å。单斜晶体属于空间群C2，a = 131.9 Å，b = 71.5 Å，c = 92.5 Å，β = 103.5°。