9FUE

Serial microseconds crystallography at ID29 using fixed-target (Si Chip): Lysozyme - with ligand GlcNAc


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.05 Å
  • R-Value Free: 0.265 
  • R-Value Work: 0.207 
  • R-Value Observed: 0.213 

Starting Model: experimental
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Ligand Structure Quality Assessment 


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Literature

Advancing macromolecular structure determination with microsecond X-ray pulses at a 4th generation synchrotron.

Orlans, J.Rose, S.L.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.

(2025) Commun Chem 8: 6-6

  • DOI: https://doi.org/10.1038/s42004-024-01404-y
  • Primary Citation of Related Structures:  
    9FTS, 9FTU, 9FTV, 9FTX, 9FTY, 9FU1, 9FUD, 9FUE, 9FUP

  • PubMed Abstract: 

    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 (SµX). After validating the use of different sample delivery methods with various model systems, we applied SµX 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. SµX, 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 SµX.


  • Organizational Affiliation

    ESRF - The European Synchrotron, 71 Avenue des Martyrs, Grenoble, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Lysozyme C129Gallus gallusMutation(s): 0 
EC: 3.2.1.17
UniProt
Find proteins for P00698 (Gallus gallus)
Explore P00698 
Go to UniProtKB:  P00698
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00698
Sequence Annotations
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  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.05 Å
  • R-Value Free: 0.265 
  • R-Value Work: 0.207 
  • R-Value Observed: 0.213 
  • Space Group: P 43 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 78.56α = 90
b = 78.56β = 90
c = 37.79γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
CrystFELdata reduction
CrystFELdata scaling
PHASERphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Not funded--

Revision History  (Full details and data files)

  • Version 1.0: 2025-01-22
    Type: Initial release