Crystallization and preliminary X-ray diffraction studies of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus.
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.
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.
C
C
Charron
F
F
Talfournier
M N
MN
Isupov
G
G
Branlant
J A
JA
Littlechild
B
B
Vitoux
A
A
Aubry
D001105:Archaea / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004795:Enzyme Stability; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
D011994:Recombinant Proteins; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases