RCSB PDB - 4OTV: Crystal structure of in cellulo Operophtera brumata CPV18

 4OTV

Crystal structure of in cellulo Operophtera brumata CPV18


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.179 
  • R-Value Work: 0.122 
  • R-Value Observed: 0.125 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted GTPClick on this verticalbar to view detailsBest fitted ATPClick on this verticalbar to view details

This is version 1.2 of the entry. See complete history


Literature

In cellulo structure determination of a novel cypovirus polyhedrin.

Axford, D.Ji, X.Stuart, D.I.Sutton, G.

(2014) Acta Crystallogr D Biol Crystallogr 70: 1435-1441

  • DOI: https://doi.org/10.1107/S1399004714004714
  • Primary Citation of Related Structures:  
    4OTS, 4OTV

  • PubMed Abstract: 

    This work demonstrates that with the use of a microfocus synchrotron beam the structure of a novel viral polyhedrin could be successfully determined from microcrystals within cells, removing the preparatory step of sample isolation and maintaining a favourable biological environment. The data obtained are of high quality, comparable to that obtained from isolated crystals, and enabled a facile structure determination. A small but significant difference is observed between the unit-cell parameters and the mosaic spread of in cellulo and isolated crystals, suggesting that even these robust crystals are adversely affected by removal from the cell.


  • Organizational Affiliation

    Diamond Light Source Ltd, Harwell Oxford, Didcot OX11 0DE, England.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Polyhedrin248Operophtera brumata cypovirus 18Mutation(s): 0 
UniProt
Find proteins for Q30C70 (Operophtera brumata cypovirus 18)
Explore Q30C70 
Go to UniProtKB:  Q30C70
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ30C70
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.179 
  • R-Value Work: 0.122 
  • R-Value Observed: 0.125 
  • Space Group: I 2 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 103.04α = 90
b = 103.04β = 90
c = 103.04γ = 90
Software Package:
Software NamePurpose
GDAdata collection
PHASERphasing
PHENIXrefinement
FastDPdata reduction
Blenddata scaling

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted GTPClick on this verticalbar to view detailsBest fitted ATPClick on this verticalbar to view details

Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-05-14
    Type: Initial release
  • Version 1.1: 2014-09-24
    Changes: Database references
  • Version 1.2: 2024-02-28
    Changes: Data collection, Database references, Derived calculations