Abstract
The structure of the Blastochloris viridis photosynthetic reaction center has been determined at 100 K by flash-freezing crystals. A data set to 2.2 A resolution provides a well determined model of the wild-type protein. Of particular interest are the position, occupancy and heterogeneity of the Q(B)-binding site. Data were also collected from a crystal frozen immediately after illumination. The data support predominant binding of Q(B) in the proximal position in both the neutral and charge-separated states.
| Original language | English |
|---|---|
| Pages (from-to) | 605-612 |
| Number of pages | 8 |
| Journal | Acta Crystallographica Section D: Biological Crystallography |
| Volume | 61 |
| Issue number | 5 |
| DOIs | |
| State | Published - May 2005 |
Keywords
- Binding Sites
- Cryoprotective Agents/chemistry
- Crystallization
- Darkness
- Freezing
- Herbicides/pharmacology
- Light
- Models, Molecular
- Photosynthesis/physiology
- Proteobacteria/metabolism
- Quinones/chemistry
- Ubiquinone/metabolism
- Water/chemistry
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