2GNU
The crystallization of reaction center from Rhodobacter sphaeroides occurs via a new route
Summary for 2GNU
| Entry DOI | 10.2210/pdb2gnu/pdb |
| Related | 1OGV 2BNP 2BNS |
| Descriptor | Reaction center protein H chain, CARDIOLIPIN, Reaction center protein L chain, ... (11 entities in total) |
| Functional Keywords | reaction centre, ubiquinone b, photosynthesis |
| Biological source | Rhodobacter sphaeroides More |
| Cellular location | Cellular chromatophore membrane; Single-pass membrane protein: P0C0Y7 Cellular chromatophore membrane; Multi-pass membrane protein: P0C0Y8 P0C0Y9 |
| Total number of polymer chains | 3 |
| Total formula weight | 99449.19 |
| Authors | Wadsten, P.,Woehri, A.B.,Snijder, A.,Katona, G.,Gardiner, A.T.,Cogdell, R.J.,Neutze, R.,Engstroem, S. (deposition date: 2006-04-11, release date: 2006-11-07, Last modification date: 2023-10-25) |
| Primary citation | Wadsten, P.,Woehri, A.B.,Snijder, A.,Katona, G.,Gardiner, A.T.,Cogdell, R.J.,Neutze, R.,Engstroem, S. Lipidic sponge phase crystallization of membrane proteins J.Mol.Biol., 364:44-53, 2006 Cited by PubMed Abstract: Bicontinuous lipidic cubic phases can be used as a host for growing crystals of membrane proteins. Since the cubic phase is stiff, handling is difficult and time-consuming. Moreover, the conventional cubic phase may interfere with the hydrophilic domains of membrane proteins due to the limited size of the aqueous pores. Here, we introduce a new crystallization method that makes use of a liquid analogue of the cubic phase, the sponge phase. This phase facilitates a considerable increase in the allowed size of aqueous domains of membrane proteins, and is easily generalised to a conventional vapour diffusion crystallisation experiment, including the use of nanoliter drop crystallization robots. The appearance of the sponge phase was confirmed by visual inspection, small-angle X-ray scattering and NMR spectroscopy. Crystals of the reaction centre from Rhodobacter sphaeroides were obtained by a conventional hanging-drop experiment, were harvested directly without the addition of lipase or cryoprotectant, and the structure was refined to 2.2 Angstroms resolution. In contrast to our earlier lipidic cubic phase reaction centre structure, the mobile ubiquinone could be built and refined. The practical advantages of the sponge phase make it a potent tool for crystallization of membrane proteins. PubMed: 17005199DOI: 10.1016/j.jmb.2006.06.043 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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