1CF2

THREE-DIMENSIONAL STRUCTURE OF D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM THE HYPERTHERMOPHILIC ARCHAEON METHANOTHERMUS FERVIDUS

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.257 
  • R-Value Work: 0.194 

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This is version 1.5 of the entry. See complete history. 


Literature

Crystallization and preliminary X-ray diffraction studies of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus.

Charron, C., Talfournier, F., Isupov, M.N., Branlant, G., Littlechild, J.A., Vitoux, B., Aubry, A.

(1999) Acta Crystallogr D Biol Crystallogr 55: 1353-1355

  • DOI: https://doi.org/10.1107/s0907444999005363
  • Primary Citation of Related Structures:  
    1CF2

  • PubMed Abstract: 

    The homotetrameric holo-D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus has been crystallized in the presence of NADP+ using the hanging-drop vapour-diffusion method. Crystals grew from a solution containing 2-methyl-2,4-pentanediol and magnesium acetate. A native data set has been collected to 2.1 A using synchrotron radiation and cryocooling. Diffraction data have been processed in the orthorhombic system (space group P21212) with unit-cell dimensions a = 136.7, b = 153.3, c = 74.9 A and one tetramer per asymmetric unit.

    • Organizational Affiliation: 

    Laboratoire de Cristallographie et Modélisation des Matériaux Minéraux et Biologiques, UPRESA CNRS 7036, Université Henri Poincaré, Nancy I, BP 239, 54506 Vandoeuvre-lès-Nancy, France.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE)A [auth P],
B [auth R],
C [auth O],
D [auth Q]		337Methanothermus fervidusMutation(s): 0 
EC: 1.2.1.12
UniProt
Find proteins for P10618 (Methanothermus fervidus)
Explore P10618 
Go to UniProtKB:  P10618
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP10618
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.257 
  • R-Value Work: 0.194 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 136.66α = 90
b = 153.28β = 90
c = 74.92γ = 90
Software Package:
Software NamePurpose
REFMACrefinement

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-03-29
    Type: Initial release
  • Version 1.1: 2008-04-26
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-04-04
    Changes: Data collection
  • Version 1.4: 2018-04-11
    Changes: Data collection
  • Version 1.5: 2023-12-27
    Changes: Data collection, Database references, Derived calculations