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 language | English (US) |
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Pages (from-to) | 1498-1505 |
Number of pages | 8 |
Journal | Acta Crystallographica Section D: Biological Crystallography |
Volume | 57 |
Issue number | 11 |
DOIs | |
State | Published - 2001 |
ASJC Scopus subject areas
- Structural Biology
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Structure of cytochrome c2 from Rhodospirillum Centenum
Camara-Artigas, A. (Contributor), Williams, J. (Contributor) & Allen, J. (Contributor), Protein Data Bank (PDB), Nov 7 2001
DOI: 10.2210/pdb1JDL, https://www.wwpdb.org/pdb?id=pdb_00001jdl
Dataset