Generic placeholder image

Protein & Peptide Letters


ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Purification, Crystallization and Preliminary Crystallographic Analysis of CYP 195A2, a P450 Enzyme from Rhodopseudomonas palustris

Author(s): Delin Guo, Feng Xu, Stephen G. Bell, Xiaoyun Pang, Mark Bartlam and Luet-Lok Wong

Volume 15, Issue 4, 2008

Page: [423 - 426] Pages: 4

DOI: 10.2174/092986608784246470

Price: $65


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 Å and 2.8 Å have been collected and processed in space groups P222 and C2221 respectively.

Keywords: Cytochrome P450, CYP195A2, Rhodopseudomonas palustris, crystallization

« Previous

Rights & Permissions Print Export Cite as
© 2023 Bentham Science Publishers | Privacy Policy