Crystallization and preliminary X-ray diffraction studies of an α-methylacyl-CoA racemase from Mycobacterium tuberculosis

被引：14
|
作者：
Bhaumik, P
Kursula, P
Ratas, V
Conzelmann, E
Hiltunen, JK
Schmitz, W
Wierenga, RK
机构：
[1] Oulu Univ, Bioctr, FIN-90014 Oulu, Finland
[2] Oulu Univ, Dept Biochem, FIN-90014 Oulu, Finland
[3] Univ Wurzburg, Biozentrum, D-97074 Wurzburg, Germany
来源：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2003年 / 59卷
关键词：
D O I：
10.1107/S0907444902020735
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
alpha-Methylacyl-CoA racemase is a key enzyme in the metabolism of 2-methyl-branched fatty acids and, in mammals, in the conversion of cholesterol to bile acids. The enzyme from Mycobacterium tuberculosis has been purified to homogeneity and crystallized by the hanging-drop vapour-diffusion method. The crystals of the un-liganded racemase belong to space group P6(1)22 or P6(5)22, with unit-cell parameters a = b = 122.0, c = 256.4 Angstrom. Data sets were collected at 100 K. The crystals diffract to 2.8 Angstrom using synchrotron radiation.
引用
收藏
页码：353 / 355
页数：3
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