Please use this identifier to cite or link to this item:
https://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: international journal for rapid publication of short papers in protein and peptide science, 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 |
DOI: | 10.2174/092986608784246470 |
Published version: | http://dx.doi.org/10.2174/092986608784246470 |
Appears in Collections: | Aurora harvest 4 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.