CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF ESCHERICHIA-COLI GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE

Authors
OLIVIER L BUISSON G FANCHON E CORBIER C BRANLANT G DIDEBERG O
Citation
L. Olivier et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF ESCHERICHIA-COLI GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE, Acta crystallographica. Section D, Biological crystallography, 51, 1995, pp. 245-247
Citations number
30
Categorie Soggetti
Crystallography,Biology,"Pharmacology & Pharmacy
Journal title
Acta crystallographica. Section D, Biological crystallography → ACNP
ISSN journal
09074449
Volume
51
Year of publication
1995
Part
2
Pages
245 - 247
Database
ISI
SICI code
0907-4449(1995)51:<245:CAPDSO>2.0.ZU;2-L
Abstract
Phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key enzyme in glycolysis. Single crystals of NAD-dependent GAPDH from Escherichia coli have been obtained by vapour diffusion at room temper ature using trisodium citrate as precipitant. In almost the same cryst allization conditions, two kinds of crystals were found to be suitable for X-ray diffraction. The crystals with only one half of a tetramer in the asymmetric unit were chosen for high-resolution analysis. They belonged to space group C222(1), with cell dimensions a = 79.1, b = 18 9.6 and c = 122.2 Angstrom. These crystals diffracted to 1.8 Angstrom resolution.