7Q7Q
LIPIDIC CUBIC PHASE SERIAL FEMTOSECOND CRYSTALLOGRAPHY STRUCTURE OF A PHOTOSYNTHETIC REACTION CENTRE
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Summary for 7Q7Q
| Entry DOI | 10.2210/pdb7q7q/pdb |
| Descriptor | Photosynthetic reaction center cytochrome c subunit, BACTERIOPHEOPHYTIN B, HEPTANE-1,2,3-TRIOL, ... (17 entities in total) |
| Functional Keywords | crystallography structure photosynthetic reaction centre, membrane protein |
| Biological source | Blastochloris viridis More |
| Total number of polymer chains | 4 |
| Total formula weight | 146924.53 |
| Authors | Baath, P.,Banacore, A.,Neutze, R. (deposition date: 2021-11-09, release date: 2022-06-22, Last modification date: 2024-10-23) |
| Primary citation | Bath, P.,Banacore, A.,Borjesson, P.,Bosman, R.,Wickstrand, C.,Safari, C.,Dods, R.,Ghosh, S.,Dahl, P.,Ortolani, G.,Bjorg Ulfarsdottir, T.,Hammarin, G.,Garcia Bonete, M.J.,Vallejos, A.,Ostojic, L.,Edlund, P.,Linse, J.B.,Andersson, R.,Nango, E.,Owada, S.,Tanaka, R.,Tono, K.,Joti, Y.,Nureki, O.,Luo, F.,James, D.,Nass, K.,Johnson, P.J.M.,Knopp, G.,Ozerov, D.,Cirelli, C.,Milne, C.,Iwata, S.,Branden, G.,Neutze, R. Lipidic cubic phase serial femtosecond crystallography structure of a photosynthetic reaction centre. Acta Crystallogr D Struct Biol, 78:698-708, 2022 Cited by PubMed Abstract: Serial crystallography is a rapidly growing method that can yield structural insights from microcrystals that were previously considered to be too small to be useful in conventional X-ray crystallography. Here, conditions for growing microcrystals of the photosynthetic reaction centre of Blastochloris viridis within a lipidic cubic phase (LCP) crystallization matrix that employ a seeding protocol utilizing detergent-grown crystals with a different crystal packing are described. LCP microcrystals diffracted to 2.25 Å resolution when exposed to XFEL radiation, which is an improvement of 0.15 Å over previous microcrystal forms. Ubiquinone was incorporated into the LCP crystallization media and the resulting electron density within the mobile Q pocket is comparable to that of other cofactors within the structure. As such, LCP microcrystallization conditions will facilitate time-resolved diffraction studies of electron-transfer reactions to the mobile quinone, potentially allowing the observation of structural changes associated with the two electron-transfer reactions leading to complete reduction of the ubiquinone ligand. PubMed: 35647917DOI: 10.1107/S2059798322004144 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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