- Abstract:
-
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 resolutio...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1107/s1744309107012705
-
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- Journal:
- Acta crystallographica. Section F, Structural biology and crystallization communications
- Volume:
- 63
- Issue:
- Pt 4
- Pages:
- 342-345
- Publication date:
- 2007-04-05
- DOI:
- EISSN:
-
1744-3091
- ISSN:
-
1744-3091
- URN:
-
uuid:34643c68-5c57-4ed5-b4d4-95ce6e130a76
- Source identifiers:
-
40348
- Local pid:
- pubs:40348
- Copyright date:
- 2007
Journal article
Purification, crystallization and preliminary crystallographic analysis of cytochrome P450 203A1 from Rhodopseudomonas palustris.
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