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

9fup is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:, , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AA2AR_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 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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. 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. Advancing macromolecular structure determination with microsecond X-ray pulses at a 4th generation synchrotron. Commun Chem. 2025 Jan 7;8(1):6. PMID:39775172 doi:10.1038/s42004-024-01404-y

9fup, resolution 2.50Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA