8RGW

Serial synchrotron in plate room temperature structure of Dye Type Peroxidase Aa, 12 drops merged


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.88 Å
  • R-Value Free: 0.242 
  • R-Value Work: 0.212 
  • R-Value Observed: 0.213 

Starting Model: experimental
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Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Efficient in situ screening of and data collection from microcrystals in crystallization plates.

Thompson, A.J.Sanchez-Weatherby, J.Williams, L.J.Mikolajek, H.Sandy, J.Worrall, J.A.R.Hough, M.A.

(2024) Acta Crystallogr D Struct Biol 80: 279-288

  • DOI: https://doi.org/10.1107/S2059798324001955
  • Primary Citation of Related Structures:  
    8RGE, 8RGS, 8RGW, 8RGY

  • PubMed Abstract: 

    A considerable bottleneck in serial crystallography at XFEL and synchrotron sources is the efficient production of large quantities of homogenous, well diffracting microcrystals. Efficient high-throughput screening of batch-grown microcrystals and the determination of ground-state structures from different conditions is thus of considerable value in the early stages of a project. Here, a highly sample-efficient methodology to measure serial crystallography data from microcrystals by raster scanning within standard in situ 96-well crystallization plates is described. Structures were determined from very small quantities of microcrystal suspension and the results were compared with those from other sample-delivery methods. The analysis of a two-dimensional batch crystallization screen using this method is also described as a useful guide for further optimization and the selection of appropriate conditions for scaling up microcrystallization.


  • Organizational Affiliation

    Diamond Light Source Ltd, Harwell Science and Innovation Campus, Didcot OX11 0DE, United Kingdom.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Deferrochelatase
A, B
373Streptomyces lividansMutation(s): 0 
Gene Names: SLI_2602
EC: 1.11.1
UniProt
Find proteins for A0A7U9DT46 (Streptomyces lividans 1326)
Explore A0A7U9DT46 
Go to UniProtKB:  A0A7U9DT46
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A7U9DT46
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.88 Å
  • R-Value Free: 0.242 
  • R-Value Work: 0.212 
  • R-Value Observed: 0.213 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 72.428α = 90
b = 67.728β = 105.69
c = 74.673γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
Cootmodel building
xia2data reduction
xia2data scaling
PHENIXphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Diamond Light SourceUnited KingdomSTU0436

Revision History  (Full details and data files)

  • Version 1.0: 2023-12-27
    Type: Initial release
  • Version 1.1: 2024-03-27
    Changes: Database references, Structure summary
  • Version 1.2: 2024-04-17
    Changes: Database references