4YCR
Structure determination of an integral membrane protein at room temperature from crystals in situ
Summary for 4YCR
| Entry DOI | 10.2210/pdb4ycr/pdb |
| Related | 3M71 |
| Descriptor | Tellurite resistance protein TehA homolog, octyl beta-D-glucopyranoside (3 entities in total) |
| Functional Keywords | in situ data collection, membrane protein, multiple datasets, synchrotron beamline |
| Biological source | Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) |
| Cellular location | Cell inner membrane ; Multi- pass membrane protein : P44741 |
| Total number of polymer chains | 1 |
| Total formula weight | 34052.11 |
| Authors | Axford, D.,Hu, N.J.,Foadi, J.,Choudhury, H.G.,Iwata, S.,Beis, K.,Evans, G.,Alguel, Y. (deposition date: 2015-02-20, release date: 2015-06-03, Last modification date: 2024-05-08) |
| Primary citation | Axford, D.,Foadi, J.,Hu, N.J.,Choudhury, H.G.,Iwata, S.,Beis, K.,Evans, G.,Alguel, Y. Structure determination of an integral membrane protein at room temperature from crystals in situ. Acta Crystallogr.,Sect.D, 71:1228-1237, 2015 Cited by PubMed Abstract: The structure determination of an integral membrane protein using synchrotron X-ray diffraction data collected at room temperature directly in vapour-diffusion crystallization plates (in situ) is demonstrated. Exposing the crystals in situ eliminates manual sample handling and, since it is performed at room temperature, removes the complication of cryoprotection and potential structural anomalies induced by sample cryocooling. Essential to the method is the ability to limit radiation damage by recording a small amount of data per sample from many samples and subsequently assembling the resulting data sets using specialized software. The validity of this procedure is established by the structure determination of Haemophilus influenza TehA at 2.3 Å resolution. The method presented offers an effective protocol for the fast and efficient determination of membrane-protein structures at room temperature using third-generation synchrotron beamlines. PubMed: 26057664DOI: 10.1107/S139900471500423X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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