6Z27
Photosynthetic Reaction Center From Rhodobacter Sphaeroides strain RV LCP crystallization
Summary for 6Z27
| Entry DOI | 10.2210/pdb6z27/pdb |
| Related | 6Z02 6Z1J |
| Descriptor | Reaction center protein H chain, UBIQUINONE-10, 1,2-ETHANEDIOL, ... (12 entities in total) |
| Functional Keywords | photosynthetic reaction center, bacteriochlorophyll, rhodobacter sphaeroides, serial crystallography, mesophase crystallization, lipid sponge phase, lipid cubic phase, spheroidene, ubiquinone, photosynthesis |
| Biological source | Rhodobacter sphaeroides More |
| Total number of polymer chains | 3 |
| Total formula weight | 101777.81 |
| Authors | Gabdulkhakov, A.G.,Fufina, T.Y.,Vasilieva, L.G.,Betzel, C.,Selikhanov, G.K. (deposition date: 2020-05-15, release date: 2020-12-02, Last modification date: 2024-01-24) |
| Primary citation | Selikhanov, G.,Fufina, T.,Vasilieva, L.,Betzel, C.,Gabdulkhakov, A. Novel approaches for the lipid sponge phase crystallization of the Rhodobacter sphaeroides photosynthetic reaction center. Iucrj, 7:1084-1091, 2020 Cited by PubMed Abstract: With the recent developments in the field of free-electron-laser-based serial femtosecond crystallography, the necessity to obtain a large number of high-quality crystals has emerged. In this work crystallization techniques were selected, tested and optimized for the lipid mesophase crystallization of the membrane pigment-protein complex, known as the photosynthetic reaction center (RC). Novel approaches for lipid sponge phase crystallization in comparatively large volumes using Hamilton gas-tight glass syringes and plastic pipetting tips are described. An analysis of RC crystal structures obtained by lipid mesophase crystallization revealed non-native ligands that displaced the native electron-transfer cofactors (carotenoid sphero-idene and a ubi-quinone molecule) from their binding pockets. These ligands were identified and were found to be lipids that are major mesophase components. The selection of distinct co-crystallization conditions with the missing cofactors facilitated the restoration of sphero-idene in its binding site. PubMed: 33209319DOI: 10.1107/S2052252520012142 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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