Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5NLX

A2A Adenosine receptor room-temperature structure determined by serial millisecond crystallography

Summary for 5NLX
Entry DOI10.2210/pdb5nlx/pdb
DescriptorAdenosine receptor A2a,Soluble cytochrome b562,Adenosine receptor A2a, OLEIC ACID, SODIUM ION, ... (6 entities in total)
Functional Keywordsroom-temperature, serial crystallography, gpcr, hydrolase, membrane protein
Biological sourceHomo sapiens (Human)
More
Cellular locationCell membrane; Multi-pass membrane protein: P29274
Total number of polymer chains1
Total formula weight50364.42
Authors
Primary citationWeinert, 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: 28912485
DOI: 10.1038/s41467-017-00630-4
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.14 Å)
Structure validation

226707

數據於2024-10-30公開中

PDB statisticsPDBj update infoContact PDBjnumon