1QC9

THE CRYSTALLOGRAPHIC STRUCTURE OF RESTRICTION ENDONUCLEASE ECO RI AT 3.3 A IN THE ABSENSE OF DNA


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.295 
  • R-Value Work: 0.251 

wwPDB Validation   3D Report Full Report


This is version 1.6 of the entry. See complete history


Literature

The 3.3 A Crystallographic Structure of Restriction Endonuclease Eco RI in the Absence of DNA

Chandrasekhar, K.Horvath, M.M.Samudzi, C.Choi, J.Rosenberg, J.M.

To be published.

Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (ECO RI ENDONUCLEASE)
A, B, C
276Escherichia coliMutation(s): 0 
EC: 3.1.21.4
UniProt
Find proteins for P00642 (Escherichia coli)
Explore P00642 
Go to UniProtKB:  P00642
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00642
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.295 
  • R-Value Work: 0.251 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 208.68α = 90
b = 127.35β = 98.57
c = 49.87γ = 90
Software Package:
Software NamePurpose
MERLOTphasing
X-PLORrefinement
X-GENdata reduction
X-GENdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-06-10
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2017-02-01
    Changes: Database references, Structure summary
  • Version 1.4: 2017-02-08
    Changes: Derived calculations
  • Version 1.5: 2017-10-04
    Changes: Refinement description
  • Version 1.6: 2024-02-14
    Changes: Data collection, Database references