2FX3

Crystal Structure Determination of E. coli Elongation Factor, Tu using a Twinned Data Set

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.40 Å
  • R-Value Free: 0.262 
  • R-Value Work: 0.197 

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This is version 1.3 of the entry. See complete history. 


Literature

Solving the structure of Escherichia coli elongation factor Tu using a twinned data set.

Heffron, S.E., Moeller, R., Jurnak, F.

(2006) Acta Crystallogr D Biol Crystallogr 62: 433-438

  • DOI: https://doi.org/10.1107/S0907444906004021
  • Primary Citation of Related Structures:  
    2FX3

  • PubMed Abstract: 

    Escherichia coli elongation factor Tu-GDP (EF-Tu-GDP) was crystallized in the presence of novel inhibitors. The only crystals which could be grown were epitaxially as well as merohedrally twinned, highly mosaic and diffracted to a resolution of 3.4 A in space group P3(1)21, with unit-cell parameters a = b = 69.55, c = 169.44 A, alpha = beta = 90, gamma = 120 degrees . To determine whether an inhibitor was present in the crystal, a poor-quality X-ray diffraction data set had to be processed. The three-dimensional structure was ultimately solved and the original question answered. The results also reveal a new type of dimer packing for EF-Tu-GDP.

    • Organizational Affiliation: 

    University of California, Irvine, USA.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Elongation factor Tu393Escherichia coliMutation(s): 0 
UniProt
Find proteins for P0CE47 (Escherichia coli (strain K12))
Explore P0CE47 
Go to UniProtKB:  P0CE47
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0CE47
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
GDP
Query on GDP
Download Ideal Coordinates CCD File 
C [auth A]GUANOSINE-5'-DIPHOSPHATE
C10 H15 N5 O11 P2
QGWNDRXFNXRZMB-UUOKFMHZSA-N
MG
Query on MG
Download Ideal Coordinates CCD File 
B [auth A]MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.40 Å
  • R-Value Free: 0.262 
  • R-Value Work: 0.197 
  • Space Group: P 31 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 69.55α = 90
b = 69.55β = 90
c = 169.44γ = 120
Software Package:
Software NamePurpose
SCALAdata scaling
PHASERphasing
CNSrefinement
PDB_EXTRACTdata extraction
MOSFLMdata reduction
CCP4data scaling

Structure Validation

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Ligand Structure Quality Assessment 


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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-03-28
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-08-30
    Changes: Data collection, Database references, Derived calculations, Refinement description