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 |
|---|---|
| Pages (from-to) | 1498-1505 |
| Number of pages | 8 |
| Journal | Acta Crystallographica Section D: Biological Crystallography |
| Volume | 57 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - 2001 |
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ASJC Scopus subject areas
- Clinical Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biophysics
- Condensed Matter Physics
- Structural Biology
Cite this
Structure of cytochrome c2 from Rhodospirillum centenum. / Camara-Artigas, A.; Williams, J. C.; Allen, James Paul.
In: Acta Crystallographica Section D: Biological Crystallography, Vol. 57, No. 11, 2001, p. 1498-1505.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Structure of cytochrome c2 from Rhodospirillum centenum
AU - Camara-Artigas, A.
AU - Williams, J. C.
AU - Allen, James Paul
PY - 2001
Y1 - 2001
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0034740291&partnerID=8YFLogxK
U2 - 10.1107/S0907444901010423
DO - 10.1107/S0907444901010423
M3 - Article
C2 - 11679712
AN - SCOPUS:0034740291
VL - 57
SP - 1498
EP - 1505
JO - Acta Crystallographica Section D: Structural Biology
JF - Acta Crystallographica Section D: Structural Biology
SN - 0907-4449
IS - 11
ER -