Purification, crystallization and preliminary crystallographic analysis of CYP 195A2, a P450 enzyme from Rhodopseudomonas palustris

Protein Pept Lett. 2008;15(4):423-6. doi: 10.2174/092986608784246470.

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

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Cytochrome P-450 Enzyme System / chemistry*
  • Cytochrome P-450 Enzyme System / isolation & purification*
  • Rhodopseudomonas / enzymology*

Substances

  • Cytochrome P-450 Enzyme System