5nm4: Difference between revisions
New page: '''Unreleased structure''' The entry 5nm4 is ON HOLD until sometime in the future Authors: Weinert, T., Cheng, R., James, D., Gashi, D., Nogly, P., Jaeger, K., Hennig, M., Standfuss, J.... |
No edit summary |
||
| (5 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
The | ==A2A Adenosine receptor room-temperature structure determined by serial femtosecond crystallography== | ||
<StructureSection load='5nm4' size='340' side='right'caption='[[5nm4]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5nm4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NM4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NM4 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</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'>[https://proteopedia.org/fgij/fg.htm?mol=5nm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nm4 OCA], [https://pdbe.org/5nm4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nm4 RCSB], [https://www.ebi.ac.uk/pdbsum/5nm4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nm4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AA2AR_HUMAN AA2AR_HUMAN] Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.[https://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX] Electron-transport protein of unknown function. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:28912485</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5nm4" style="background-color:#fffaf0;"></div> | ||
[[Category: Cheng | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Adenosine A2A receptor 3D structures|Adenosine A2A receptor 3D structures]] | ||
[[Category: Jaeger | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Escherichia coli]] | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Cheng R]] | |||
[[Category: Gashi D]] | |||
[[Category: Hennig M]] | |||
[[Category: Jaeger K]] | |||
[[Category: James D]] | |||
[[Category: Nogly P]] | |||
[[Category: Standfuss J]] | |||
[[Category: Weinert T]] | |||