Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/75973
Citations
Scopus Web of Science® Altmetric
?
?
Type: Journal article
Title: Purification, crystallization and preliminary crystallographic analysis of CYP195A2, a P450 enzyme from Rhodopseudomonas palustris
Author: Guo, D.
Xu, F.
Bell, S.
Pang, X.
Bartlam, M.
Wong, L.
Citation: Protein and Peptide Letters, 2008; 15(4):423-426
Publisher: Bentham Science Publ Ltd
Issue Date: 2008
ISSN: 0929-8665
1875-5305
Statement of
Responsibility: 
Delin Guo, Feng Xu, Stephen G. Bell, Xiaoyun Pang, Mark Bartlam and Luet-Lok Wong
Abstract: 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
Rights: Copyright status unknown
RMID: 0020121295
DOI: 10.2174/092986608784246470
Appears in Collections:Chemistry and Physics publications

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.