Structure of cytochrome c2 from Rhodospirillum centenum

A. Camara-Artigas, Joann Williams, James Allen

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Cytochrome c2 from the purple photosynthetic bacterium Rhodospirillum centenum has been crystallized by the sitting-drop vapour-diffusion method. The crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 29.7, b = 59.9, c = 65.4 Å, and diffract to a resolution limit of 1.7 Å. The Fe-atom position was determined from its anomalous scattering contribution and a molecular-replacement solution was calculated. The correctness of the solution was confirmed by parallel isomorphous replacement studies. The resulting model has a type I cytochrome fold with two features, an extended α-helix and a surface-charge distribution, that are distinctive to this protein. The implications of these structural features for the ability of the cytochrome to serve as an electron carrier are discussed.

Original languageEnglish (US)
Pages (from-to)1498-1505
Number of pages8
JournalActa Crystallographica Section D: Biological Crystallography
Volume57
Issue number11
DOIs
StatePublished - Nov 20 2001

ASJC Scopus subject areas

  • Structural Biology

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