5NLX
A2A Adenosine receptor room-temperature structure determined by serial millisecond crystallography
Summary for 5NLX
Entry DOI | 10.2210/pdb5nlx/pdb |
Descriptor | Adenosine receptor A2a,Soluble cytochrome b562,Adenosine receptor A2a, OLEIC ACID, SODIUM ION, ... (6 entities in total) |
Functional Keywords | room-temperature, serial crystallography, gpcr, hydrolase, membrane protein |
Biological source | Homo sapiens (Human) More |
Cellular location | Cell membrane; Multi-pass membrane protein: P29274 |
Total number of polymer chains | 1 |
Total formula weight | 50364.42 |
Authors | Weinert, T.,Cheng, R.,James, D.,Gashi, D.,Nogly, P.,Jaeger, K.,Dore, A.S.,Geng, T.,Cooke, R.,Hennig, M.,Standfuss, J. (deposition date: 2017-04-05, release date: 2017-09-27) |
Primary citation | Weinert, T.,Olieric, N.,Cheng, R.,Brunle, S.,James, D.,Ozerov, D.,Gashi, D.,Vera, L.,Marsh, M.,Jaeger, K.,Dworkowski, F.,Panepucci, E.,Basu, S.,Skopintsev, P.,Dore, A.S.,Geng, T.,Cooke, R.M.,Liang, M.,Prota, A.E.,Panneels, V.,Nogly, P.,Ermler, U.,Schertler, G.,Hennig, M.,Steinmetz, M.O.,Wang, M.,Standfuss, J. Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons. Nat Commun, 8:542-542, 2017 Cited by PubMed Abstract: Historically, room-temperature structure determination was succeeded by cryo-crystallography to mitigate radiation damage. Here, we demonstrate that serial millisecond crystallography at a synchrotron beamline equipped with high-viscosity injector and high frame-rate detector allows typical crystallographic experiments to be performed at room-temperature. Using a crystal scanning approach, we determine the high-resolution structure of the radiation sensitive molybdenum storage protein, demonstrate soaking of the drug colchicine into tubulin and native sulfur phasing of the human G protein-coupled adenosine receptor. Serial crystallographic data for molecular replacement already converges in 1,000-10,000 diffraction patterns, which we collected in 3 to maximally 82 minutes. Compared with serial data we collected at a free-electron laser, the synchrotron data are of slightly lower resolution, however fewer diffraction patterns are needed for de novo phasing. Overall, the data we collected by room-temperature serial crystallography are of comparable quality to cryo-crystallographic data and can be routinely collected at synchrotrons.Serial crystallography was developed for protein crystal data collection with X-ray free-electron lasers. Here the authors present several examples which show that serial crystallography using high-viscosity injectors can also be routinely employed for room-temperature data collection at synchrotrons. PubMed: 28912485DOI: 10.1038/s41467-017-00630-4 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.14 Å) |
Structure validation
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