Crystallization and preliminary X-ray diffraction analysis of the di-haem cytochrome c peroxidase from Pseudomonas stutzeri

Acta Crystallogr D Biol Crystallogr. 2003 Feb;59(Pt 2):345-7. doi: 10.1107/s0907444902020760. Epub 2003 Jan 23.

Abstract

Crystals of cytochrome c peroxidase from Pseudomonas stutzeri were obtained using sodium citrate and PEG 8000 as precipitants. A complete data set was collected to a resolution of 1.6 A under cryogenic conditions using synchrotron radiation at the ESRF. The crystals belong to space group P2(1), with unit-cell parameters a = 69.29, b = 143.31, c = 76.83 A, beta = 100.78 degrees. Four CCP molecules were found in the asymmetric unit, corresponding to a pair of dimers related by local dyads. The crystal packing in the structure shows that the functional dimers can dimerize, as suggested by previous biochemical studies.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization / methods
  • Crystallography, X-Ray
  • Cytochrome-c Peroxidase / chemistry*
  • Dimerization
  • Heme / chemistry*
  • Models, Molecular
  • Pseudomonas / enzymology*
  • Synchrotrons

Substances

  • Heme
  • Cytochrome-c Peroxidase