Purification, crystallization and preliminary crystallographic analysis of CYP 195A2, a P450 enzyme from Rhodopseudomonas palustris.
Cytochrome P450 monooxygenases are a superfamily of heme-thiolate proteins involved in the metabolism of a wide variety of endogenous and xenobiotic compounds. The P450 enzyme CYP195A2 from Rhodopseudomonas palustris CGA009, a metabolically versatile bacterium, was overproduced in E. coli and purified. Two distinct crystal forms were obtained under separately optimized conditions by the hanging-drop vapor-diffusion method. Native data sets extending to resolutions of 2.3 A and 2.8 A have been collected and processed in space groups P222 and C2221 respectively.
Guo
Delin
D
Laboratory of Structural Biology, School of Medicine, Tsinghua University, Beijing, 100084, China.
Xu
Feng
F
Bell
Stephen G
SG
Pang
Xiaoyun
X
Bartlam
Mark
M
Wong
Luet-Lok
LL
D003460:Crystallization; D018360:Crystallography, X-Ray; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000302:isolation & purification*; D012241:Rhodopseudomonas / Q000201:enzymology*
D003577:Cytochrome P-450 Enzyme System