9D2H

Stigmatella aurantica bacteriophytochrome protein 2 (SaBphP2), photosensory core module, investigated at ESRF(EBS) ID29. Dark Structure.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.261 
  • R-Value Work: 0.192 
  • R-Value Observed: 0.195 

Starting Model: experimental
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Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

Exploiting fourth-generation synchrotron radiation for enzyme and photoreceptor characterization.

Malla, T.N.Muniyappan, S.Menendez, D.Ogukwe, F.Dale, A.N.Clayton, J.D.Weatherall, D.D.Karki, P.Dangi, S.Mandella, V.Pacheco, A.A.Stojkovic, E.A.Rose, S.L.Orlans, J.Basu, S.de Sanctis, D.Schmidt, M.

(2025) IUCrJ 12: 36-48

  • DOI: https://doi.org/10.1107/S2052252524010868
  • Primary Citation of Related Structures:  
    9CUF, 9D10, 9D2H

  • PubMed Abstract: 

    The upgrade of the European Synchrotron Radiation Facility (ESRF) in Grenoble, France to an Extremely Brilliant Source (EBS) is expected to enable time-resolved synchrotron serial crystallography (SSX) experiments with sub-millisecond time resolution. ID29 is a new beamline dedicated to SSX experiments at ESRF-EBS. Here, we report experiments emerging from the initial phase of user operation at ID29. We first used microcrystals of photoactive yellow protein as a model system to exploit the potential of microsecond pulses for SSX. Subsequently, we investigated microcrystals of cytochrome c nitrite reductase (ccNiR) with microsecond X-ray pulses. CcNiR is a decaheme protein that is ideal for the investigation of radiation damage at the various heme-iron sites. Finally, we performed a proof-of-concept subsecond time-resolved SSX experiment by photoactivating microcrystals of a myxobacterial phytochrome.


  • Organizational Affiliation

    Department of Physics, University of Wisconsin-Milwaukee, Milwaukee, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
histidine kinase
A, B
490Stigmatella aurantiacaMutation(s): 0 
Gene Names: STIAU_8420
EC: 2.7.13.3
UniProt
Find proteins for Q09E27 (Stigmatella aurantiaca (strain DW4/3-1))
Explore Q09E27 
Go to UniProtKB:  Q09E27
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ09E27
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.261 
  • R-Value Work: 0.192 
  • R-Value Observed: 0.195 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 83.69α = 90
b = 83.4β = 107.63
c = 86.87γ = 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
National Science Foundation (NSF, United States)United States1231306
National Science Foundation (NSF, United States)United States2423601

Revision History  (Full details and data files)

  • Version 1.0: 2025-01-15
    Type: Initial release
  • Version 1.1: 2025-01-22
    Changes: Database references