5G26

Unveiling the Mechanism Behind the in-meso Crystallization of Membrane Proteins


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.42 Å
  • R-Value Free: 0.278 
  • R-Value Work: 0.222 
  • R-Value Observed: 0.224 

Starting Model: experimental
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Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

The Nanoscience Behind the Art of in-Meso Crystallization of Membrane Proteins.

Zabara, A.Meikle, T.G.Newman, J.Peat, T.S.Conn, C.E.Drummond, C.J.

(2017) Nanoscale 9: 754

  • DOI: https://doi.org/10.1039/c6nr07634c
  • Primary Citation of Related Structures:  
    5G26

  • PubMed Abstract: 

    The structural changes occurring at the nanoscale level within the lipid bilayer and driving the in-meso formation of large well-diffracting membrane protein crystals have been uniquely characterized for a model membrane protein, intimin. Importantly, the order to order transitions taking place within the bilayer and the lipidic nanostructures required for crystal growth have been shown to be general, occurring for both the cubic and the sponge mesophase crystallization pathways. For the first time, a transient fluid lamellar phase has been observed and unambiguously assigned for both crystallization pathways, present at the earliest stages of protein crystallogenesis but no longer observed once the crystals surpass the size of the average lyotropic liquid crystalline domain. The reported time-resolved structural investigation provides a significantly improved and general understanding of the nanostructural changes taking place within the mesophase during in-meso crystallization which is a fundamental advance in the enabling area of membrane protein structural biology.


  • Organizational Affiliation

    RMIT University, School of Science, College of Science Engineering and Health 124 La Trobe Street, Melbourne, Victoria 3000, Australia. [email protected] and Biomedical Manufacturing Program, Commonwealth Scientific and Industrial Research Organisation (CSIRO), 343 Royal Parade, Parkville, Victoria 3052, Australia.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
INTIMIN242Escherichia coli O157Mutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for P43261 (Escherichia coli O157:H7)
Explore P43261 
Go to UniProtKB:  P43261
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP43261
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.42 Å
  • R-Value Free: 0.278 
  • R-Value Work: 0.222 
  • R-Value Observed: 0.224 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 115.944α = 90
b = 119.925β = 90
c = 39.043γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2017-02-15
    Type: Initial release
  • Version 1.1: 2024-01-10
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description