6FMX

IMISX-EP of W-PgpB


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.79 Å
  • R-Value Free: 0.262 
  • R-Value Work: 0.237 
  • R-Value Observed: 0.238 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

In situ serial crystallography for rapid de novo membrane protein structure determination.

Huang, C.Y.Olieric, V.Howe, N.Warshamanage, R.Weinert, T.Panepucci, E.Vogeley, L.Basu, S.Diederichs, K.Caffrey, M.Wang, M.

(2018) Commun Biol 1: 124-124

  • DOI: https://doi.org/10.1038/s42003-018-0123-6
  • Primary Citation of Related Structures:  
    6FMR, 6FMS, 6FMT, 6FMV, 6FMW, 6FMX, 6FMY

  • PubMed Abstract: 

    De novo membrane protein structure determination is often limited by the availability of large crystals and the difficulties in obtaining accurate diffraction data for experimental phasing. Here we present a method that combines in situ serial crystallography with de novo phasing for fast, efficient membrane protein structure determination. The method enables systematic diffraction screening and rapid data collection from hundreds of microcrystals in in meso crystallization wells without the need for direct crystal harvesting. The requisite data quality for experimental phasing is achieved by accumulating diffraction signals from isomorphous crystals identified post-data collection. The method works in all experimental phasing scenarios and is particularly attractive with fragile, weakly diffracting microcrystals. The automated serial data collection approach can be readily adopted at most microfocus macromolecular crystallography beamlines.


  • Organizational Affiliation

    Swiss Light Source, Paul Scherrer Institute, CH-5232, Villigen, Switzerland.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Phosphatidylglycerophosphatase B222Bacillus subtilis subsp. subtilis str. 168Mutation(s): 0 
Gene Names: pgpByodMBSU19650
EC: 3.1.3.27
Membrane Entity: Yes 
UniProt
Find proteins for O34349 (Bacillus subtilis (strain 168))
Explore O34349 
Go to UniProtKB:  O34349
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO34349
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.79 Å
  • R-Value Free: 0.262 
  • R-Value Work: 0.237 
  • R-Value Observed: 0.238 
  • Space Group: I 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 68.757α = 90
b = 76.801β = 90
c = 98.912γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XSCALEdata scaling
SHELXCDphasing
SHELXDEphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Science Foundation IrelandIreland16/IA/4435
European UnionSwitzerland701647

Revision History  (Full details and data files)

  • Version 1.0: 2018-09-05
    Type: Initial release
  • Version 1.1: 2018-10-10
    Changes: Data collection, Database references, Structure summary
  • Version 1.2: 2024-05-08
    Changes: Data collection, Database references, Refinement description, Structure summary