3J7B

Catalase solved at 3.2 Angstrom resolution by MicroED


Experimental Data Snapshot

  • Method: ELECTRON CRYSTALLOGRAPHY
  • Resolution: 3.20 Å
  • R-Value Free: 0.308 
  • R-Value Work: 0.262 
  • R-Value Observed: 0.264 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structure of catalase determined by MicroED.

Nannenga, B.L.Shi, D.Hattne, J.Reyes, F.E.Gonen, T.

(2014) Elife 3: e03600-e03600

  • DOI: https://doi.org/10.7554/eLife.03600
  • Primary Citation of Related Structures:  
    3J7B

  • PubMed Abstract: 

    MicroED is a recently developed method that uses electron diffraction for structure determination from very small three-dimensional crystals of biological material. Previously we used a series of still diffraction patterns to determine the structure of lysozyme at 2.9 Å resolution with MicroED (Shi et al., 2013). Here we present the structure of bovine liver catalase determined from a single crystal at 3.2 Å resolution by MicroED. The data were collected by continuous rotation of the sample under constant exposure and were processed and refined using standard programs for X-ray crystallography. The ability of MicroED to determine the structure of bovine liver catalase, a protein that has long resisted atomic analysis by traditional electron crystallography, demonstrates the potential of this method for structure determination.


  • Organizational Affiliation

    Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, United States.


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

Unit Cell:
Length ( Å )Angle ( ˚ )
a = 67.842α = 90
b = 172.081β = 90
c = 182.067γ = 90
Software Package:
Software NamePurpose
REFMACrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-10-08
    Type: Initial release
  • Version 1.1: 2015-04-08
    Changes: Other
  • Version 1.2: 2022-08-24
    Changes: Data collection, Database references, Derived calculations
  • Version 1.3: 2024-02-21
    Changes: Data collection