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

Authors: Guo, Delin; Xu, Feng; Bell, Stephen G.; Pang, Xiaoyun; Bartlam, Mark; Wong, Luet-Lok

Source: Protein and Peptide Letters, Volume 15, Number 4, May 2008 , pp. 423-426(4)

Publisher: Bentham Science Publishers

Buy & download fulltext article:


Price: $63.10 plus tax (Refund Policy)


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: CYP195A2; Cytochrome P450; Rhodopseudomonas palustris; crystallization

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986608784246470

Publication date: May 1, 2008

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
Related content



Free Content
Free content
New Content
New content
Open Access Content
Open access content
Subscribed Content
Subscribed content
Free Trial Content
Free trial content

Text size:

A | A | A | A
Share this item with others: These icons link to social bookmarking sites where readers can share and discover new web pages. print icon Print this page