2G4O

anomalous substructure of 3-ISOPROPYLMALATE DEHYDROGENASE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.260 
  • R-Value Work: 0.209 
  • R-Value Observed: 0.210 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths.

Mueller-Dieckmann, C.Panjikar, S.Schmidt, A.Mueller, S.Kuper, J.Geerlof, A.Wilmanns, M.Singh, R.K.Tucker, P.A.Weiss, M.S.

(2007) Acta Crystallogr D Biol Crystallogr 63: 366-380

  • DOI: https://doi.org/10.1107/S0907444906055624
  • Primary Citation of Related Structures:  
    2G4H, 2G4I, 2G4J, 2G4K, 2G4L, 2G4M, 2G4N, 2G4O, 2G4P, 2G4Q, 2G4R, 2G4S, 2G4T, 2G4U, 2G4V, 2G4W, 2G4X, 2G4Y, 2G4Z, 2G51, 2G52, 2G55, 2ILL

  • PubMed Abstract: 

    23 different crystal forms of 19 different biological macromolecules were examined with respect to their anomalously scattering substructures using diffraction data collected at a wavelength of 2.0 A (6.2 keV). In more than 90% of the cases the substructure was found to contain more than just the protein S atoms. The data presented suggest that chloride, sulfate, phosphate or metal ions from the buffer or even from the purification protocol are frequently bound to the protein molecule and that these ions are often overlooked, especially if they are not bound at full occupancy. Thus, in order to fully describe the macromolecule under study, it seems desirable that any structure determination be complemented with a long-wavelength data set.


  • Organizational Affiliation

    EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
3-isopropylmalate dehydrogenase
A, B, C, D
337Mycobacterium tuberculosisMutation(s): 0 
Gene Names: leuB
EC: 1.1.1.85
UniProt
Find proteins for P9WKK9 (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))
Explore P9WKK9 
Go to UniProtKB:  P9WKK9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP9WKK9
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.260 
  • R-Value Work: 0.209 
  • R-Value Observed: 0.210 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 78.57α = 90
b = 98.58β = 90
c = 184.03γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
DENZOdata reduction
CCP4data scaling
FFTphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-02-20
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.3: 2024-02-14
    Changes: Data collection, Database references, Derived calculations