4X32
Bacteriorhodopsin ground state structure collected in cryo conditions from crystals obtained in LCP with PEG as a precipitant.
Summary for 4X32
| Entry DOI | 10.2210/pdb4x32/pdb |
| Descriptor | Bacteriorhodopsin, RETINAL, 1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL, ... (4 entities in total) |
| Functional Keywords | light-driven proton pump, retinal binding, seven transmembrane helix protein, proton transport |
| Biological source | Halobacterium salinarum |
| Cellular location | Cell membrane; Multi-pass membrane protein: P02945 |
| Total number of polymer chains | 1 |
| Total formula weight | 30388.01 |
| Authors | Nogly, P.,Standfuss, J. (deposition date: 2014-11-27, release date: 2015-02-18, Last modification date: 2024-11-13) |
| Primary citation | Nogly, P.,James, D.,Wang, D.,White, T.A.,Zatsepin, N.,Shilova, A.,Nelson, G.,Liu, H.,Johansson, L.,Heymann, M.,Jaeger, K.,Metz, M.,Wickstrand, C.,Wu, W.,Bath, P.,Berntsen, P.,Oberthuer, D.,Panneels, V.,Cherezov, V.,Chapman, H.,Schertler, G.,Neutze, R.,Spence, J.,Moraes, I.,Burghammer, M.,Standfuss, J.,Weierstall, U. Lipidic cubic phase serial millisecond crystallography using synchrotron radiation. Iucrj, 2:168-176, 2015 Cited by PubMed Abstract: Lipidic cubic phases (LCPs) have emerged as successful matrixes for the crystallization of membrane proteins. Moreover, the viscous LCP also provides a highly effective delivery medium for serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs). Here, the adaptation of this technology to perform serial millisecond crystallography (SMX) at more widely available synchrotron microfocus beamlines is described. Compared with conventional microcrystallography, LCP-SMX eliminates the need for difficult handling of individual crystals and allows for data collection at room temperature. The technology is demonstrated by solving a structure of the light-driven proton-pump bacteriorhodopsin (bR) at a resolution of 2.4 Å. The room-temperature structure of bR is very similar to previous cryogenic structures but shows small yet distinct differences in the retinal ligand and proton-transfer pathway. PubMed: 25866654DOI: 10.1107/S2052252514026487 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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