Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.7
Classification:ELECTRON TRANSPORT
Release Date:2001-11-07
Deposition Date:2001-06-14
Revision Date:2008-04-27#2011-07-13
Molecular Weight:13669.23
Macromolecule Type:Protein
Residue Count:121
Atom Site Count:935
DOI:10.2210/pdb1jdl/pdb
Abstract:
Cytochrome c(2) 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 P2(1)2(1)2(1), with unit-cell parameters a = 29.7, b = 59.9, c = 65.4 A, and diffract to a resolution limit of 1.7 A. 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 alpha-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.
Resolution:1.7
Classification:ELECTRON TRANSPORT
Release Date:2001-11-07
Deposition Date:2001-06-14
Revision Date:2008-04-27#2011-07-13
Molecular Weight:13669.23
Macromolecule Type:Protein
Residue Count:121
Atom Site Count:935
DOI:10.2210/pdb1jdl/pdb
Abstract:
Cytochrome c(2) 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 P2(1)2(1)2(1), with unit-cell parameters a = 29.7, b = 59.9, c = 65.4 A, and diffract to a resolution limit of 1.7 A. 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 alpha-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.
| Date made available | 2001 |
|---|---|
| Publisher | RCSB-PDB |
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