5nlx: Difference between revisions
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==A2A Adenosine receptor room-temperature structure determined by serial millisecond crystallography== | ==A2A Adenosine receptor room-temperature structure determined by serial millisecond crystallography== | ||
<StructureSection load='5nlx' size='340' side='right' caption='[[5nlx]], [[Resolution|resolution]] 2.14Å' scene=''> | <StructureSection load='5nlx' size='340' side='right'caption='[[5nlx]], [[Resolution|resolution]] 2.14Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5nlx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NLX OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5nlx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NLX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5NLX FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=ZMA:4-{2-[(7-AMINO-2-FURAN-2-YL[1,2,4]TRIAZOLO[1,5-A][1,3,5]TRIAZIN-5-YL)AMINO]ETHYL}PHENOL'>ZMA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=ZMA:4-{2-[(7-AMINO-2-FURAN-2-YL[1,2,4]TRIAZOLO[1,5-A][1,3,5]TRIAZIN-5-YL)AMINO]ETHYL}PHENOL'>ZMA</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5nlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nlx OCA], [http://pdbe.org/5nlx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nlx RCSB], [http://www.ebi.ac.uk/pdbsum/5nlx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nlx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| Line 18: | Line 18: | ||
</div> | </div> | ||
<div class="pdbe-citations 5nlx" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5nlx" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Adenosine A2A receptor 3D structures|Adenosine A2A receptor 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Cheng, R]] | [[Category: Cheng, R]] | ||
[[Category: Cooke, R]] | [[Category: Cooke, R]] | ||
Revision as of 15:07, 26 August 2020
A2A Adenosine receptor room-temperature structure determined by serial millisecond crystallographyA2A Adenosine receptor room-temperature structure determined by serial millisecond crystallography
Structural highlights
Function[AA2AR_HUMAN] Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. Publication Abstract from PubMedHistorically, 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. Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons.,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 AS, Geng T, Cooke RM, Liang M, Prota AE, Panneels V, Nogly P, Ermler U, Schertler G, Hennig M, Steinmetz MO, Wang M, Standfuss J Nat Commun. 2017 Sep 14;8(1):542. doi: 10.1038/s41467-017-00630-4. PMID:28912485[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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