Purification, crystallization and preliminary crystallographic analysis of cytochrome P450 203A1 from Rhodopseudomonas palustris.
Cytochrome P450 enzymes constitute a large family of haemoproteins that catalyze the monooxygenation of a great variety of endogenous and exogenous organic compounds. Cytochrome P450 203A1 (CYP203A1, RPA1009) from the metabolically versatile organism Rhodopseudomonas palustris binds a broad range of substrates, in particular substituted aromatic compounds. Crystals of CYP203A1 suitable for X-ray crystallography have been obtained and diffraction data were collected in-house to 2.0 A resolution from a single crystal. The crystals belong to space group P222, with unit-cell parameters a = 40.1, b = 95.1, c = 99.0 A, alpha = beta = gamma = 90 degrees. There is one protein molecule per asymmetric unit.
Pang
Xiaoyun
X
Laboratory of Structural Biology, School of Medicine, Tsinghua University, Beijing 100084, People's Republic of China.
Xu
Feng
F
Bell
Stephen G
SG
Guo
Delin
D
Wong
Luet Lok
LL
Rao
Zihe
Z
D000595:Amino Acid Sequence; D002846:Chromatography, Affinity; D003460:Crystallization; D018360:Crystallography, X-Ray; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D012241:Rhodopseudomonas / Q000201:enzymology*
D003577:Cytochrome P-450 Enzyme System