9fup: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
The | ==Serial microseconds crystallography at ID29 using fixed-target (small foils): A2a adenosine receptor co-crystallised with Istradefylline== | ||
<StructureSection load='9fup' size='340' side='right'caption='[[9fup]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9fup]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9FUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9FUP 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]] 2.5Å</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=JQ9:8-[(~{E})-2-(3,4-dimethoxyphenyl)ethenyl]-1,3-diethyl-7-methyl-purine-2,6-dione'>JQ9</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=OLB:(2S)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLB</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</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=9fup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9fup OCA], [https://pdbe.org/9fup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9fup RCSB], [https://www.ebi.ac.uk/pdbsum/9fup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9fup 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 == | |||
Serial macromolecular crystallography has become a powerful method to reveal room temperature structures of biological macromolecules and perform time-resolved studies. ID29, a flagship beamline of the ESRF 4th generation synchrotron, is the first synchrotron beamline in the world capable of delivering high brilliance microsecond X-ray pulses at high repetition rate for the structure determination of biological macromolecules at room temperature. The cardinal combination of microsecond exposure times, innovative beam characteristics and adaptable sample environment provides high quality complete data, even from an exceptionally small amount of crystalline material, enabling what we collectively term serial microsecond crystallography (SmicroX). After validating the use of different sample delivery methods with various model systems, we applied SmicroX to an integral membrane receptor, where only a few thousands diffraction images were sufficient to obtain a fully interpretable electron density map for the antagonist istradefylline-bound A(2A) receptor conformation, providing access to the antagonist binding mode. SmicroX, as demonstrated at ID29, will quickly find its broad applicability at upcoming 4th generation synchrotron sources worldwide and opens a new frontier in time-resolved SmicroX. | |||
Advancing macromolecular structure determination with microsecond X-ray pulses at a 4th generation synchrotron.,Orlans J, Rose SL, Ferguson G, Oscarsson M, Homs Puron A, Beteva A, Debionne S, Theveneau P, Coquelle N, Kieffer J, Busca P, Sinoir J, Armijo V, Lopez Marrero M, Felisaz F, Papp G, Gonzalez H, Caserotto H, Dobias F, Gigmes J, Lebon G, Basu S, de Sanctis D Commun Chem. 2025 Jan 7;8(1):6. doi: 10.1038/s42004-024-01404-y. PMID:39775172<ref>PMID:39775172</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9fup" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Basu S]] | |||
[[Category: Ferguson G]] | |||
[[Category: Lebon G]] | |||
[[Category: Orlans J]] | |||
[[Category: Rose SL]] | |||
[[Category: De Sanctis D]] | |||
Latest revision as of 13:22, 22 January 2025
Serial microseconds crystallography at ID29 using fixed-target (small foils): A2a adenosine receptor co-crystallised with IstradefyllineSerial microseconds crystallography at ID29 using fixed-target (small foils): A2a adenosine receptor co-crystallised with Istradefylline
Structural highlights
FunctionAA2AR_HUMAN Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.C562_ECOLX Electron-transport protein of unknown function. Publication Abstract from PubMedSerial macromolecular crystallography has become a powerful method to reveal room temperature structures of biological macromolecules and perform time-resolved studies. ID29, a flagship beamline of the ESRF 4th generation synchrotron, is the first synchrotron beamline in the world capable of delivering high brilliance microsecond X-ray pulses at high repetition rate for the structure determination of biological macromolecules at room temperature. The cardinal combination of microsecond exposure times, innovative beam characteristics and adaptable sample environment provides high quality complete data, even from an exceptionally small amount of crystalline material, enabling what we collectively term serial microsecond crystallography (SmicroX). After validating the use of different sample delivery methods with various model systems, we applied SmicroX to an integral membrane receptor, where only a few thousands diffraction images were sufficient to obtain a fully interpretable electron density map for the antagonist istradefylline-bound A(2A) receptor conformation, providing access to the antagonist binding mode. SmicroX, as demonstrated at ID29, will quickly find its broad applicability at upcoming 4th generation synchrotron sources worldwide and opens a new frontier in time-resolved SmicroX. Advancing macromolecular structure determination with microsecond X-ray pulses at a 4th generation synchrotron.,Orlans J, Rose SL, Ferguson G, Oscarsson M, Homs Puron A, Beteva A, Debionne S, Theveneau P, Coquelle N, Kieffer J, Busca P, Sinoir J, Armijo V, Lopez Marrero M, Felisaz F, Papp G, Gonzalez H, Caserotto H, Dobias F, Gigmes J, Lebon G, Basu S, de Sanctis D Commun Chem. 2025 Jan 7;8(1):6. doi: 10.1038/s42004-024-01404-y. PMID:39775172[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||