5GKN

Catalase structure determined by electron crystallography of thin 3D crystals


Experimental Data Snapshot

  • Method: ELECTRON CRYSTALLOGRAPHY
  • Resolution: 3.20 Å
  • R-Value Free: 0.304 
  • R-Value Work: 0.251 
  • R-Value Observed: 0.252 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Refinement of Cryo-EM Structures Using Scattering Factors of Charged Atoms

Yonekura, K.Maki-Yonekura, M.

(2016) J Appl Crystallogr 49: 1517-1523


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Catalase
A, B, C, D
527Bos taurusMutation(s): 0 
EC: 1.11.1.6
UniProt
Find proteins for P00432 (Bos taurus)
Explore P00432 
Go to UniProtKB:  P00432
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00432
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON CRYSTALLOGRAPHY
  • Resolution: 3.20 Å
  • R-Value Free: 0.304 
  • R-Value Work: 0.251 
  • R-Value Observed: 0.252 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 69α = 90
b = 173.5β = 90
c = 206γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
EDINTdata scaling
Modified version of phenixphasing
Modifiedphasing

Structure Validation

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Entry History & Funding Information

Deposition Data

  • Released Date: 2016-10-26 
  • Deposition Author(s): Yonekura, K.
  • This entry supersedes: 3J7U

Funding OrganizationLocationGrant Number
Japan--

Revision History  (Full details and data files)

  • Version 1.0: 2016-10-26
    Type: Initial release
  • Version 1.1: 2023-11-08
    Changes: Data collection, Database references, Derived calculations, Refinement description