CRYSTALLIZATION OF THE GLUTAMATE-DEHYDROGENASE FROM THE HYPERTHERMOPHILIC ARCHAEON THERMOCOCCUS-LITORALIS

Citation
Se. Sedelnikova et al., CRYSTALLIZATION OF THE GLUTAMATE-DEHYDROGENASE FROM THE HYPERTHERMOPHILIC ARCHAEON THERMOCOCCUS-LITORALIS, Acta crystallographica. Section D, Biological crystallography, 52, 1996, pp. 1185-1187
Citations number
9
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biology
ISSN journal
0907-4449
Volume
52
Year of publication
1996
Part
6
Pages
1185 - 1187
Database
ISI
SICI code
0907-4449(1996)52:<1185:COTGFT>2.0.ZU;2-H
Abstract
The NADP(+)-dependent glutamate dehydrogenase from Thermococcus litora lis has been crystallized by the hanging-drop method of vapour diffusi on using an ammonium sulfate and PEG mixture as the precipitant. The c rystals belong to the monoclinic System and are in space group C2 with unit-cell dimensions a = 142.7, b = 202.0, c = 125.8 Angstrom with be ta = 113.1 degrees with a hexamer in the asymmetric unit. T. Litoralis , a hyperthermophilic organism, belongs to the family of Archaea and h as a maximum growth temperature of about 370 K. The glutamate dehydrog enase isolated from this organism has a half-life of 2 h at 373 K and a comparison of this structure with that of other GluDH's from hyperth ermophilic organisms and from mesophiles will contribute to an underst anding of the molecular mechanisms which underlie thermostability.