Open AccessPurification, crystallization and preliminary crystallographic analysis of cytochrome P450 203A1 from Rhodopseudomonas palustris
Author(s) -
Pang Xiaoyun,
Bell Stephen G.,
Xu Feng,
Guo Delin,
Rao Zihe,
Wong LuetLok
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107012705
Subject(s) - rhodopseudomonas palustris , crystallization , crystallography , chemistry , cytochrome , biology , biochemistry , organic chemistry , bacteria , enzyme , genetics
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 Å resolution from a single crystal. The crystals belong to space group P 222, with unit‐cell parameters a = 40.1, b = 95.1, c = 99.0 Å, α = β = γ = 90°. There is one protein molecule per asymmetric unit.