Towards the crystal structure of glycerol dehydrogenase from Thermotoga maritima.
The NAD(+)-dependent glycerol dehydrogenase (EC 1.1.1.6) from the extremely thermophilic bacterium Thermotoga maritima has been crystallized in the presence of glycerol by the hanging-drop vapour-diffusion method using 2-methyl-2,4-pentanediol (MPD) as the precipitating agent. Crystals of the enzyme complexed with NAD(+) have also been obtained. The crystals belong to the tetragonal system with space group I422 and unit-cell parameters a = 105.3, c = 134.5 A. They diffract to a maximum resolution of 1.4 A using synchrotron radiation (lambda = 0.838 A). Crystals of the enzyme-NAD(+) complex diffract to 2.5 A resolution using in-house Cu Kalpha radiation.
Srinivasan
Vasundara
V
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA.
Ma
Kesen
K
Adams
Michael W W
MW
Newton
M Gary
MG
Rose
John P
JP
Wang
Bi Cheng
BC
D018360:Crystallography, X-Ray; D011487:Protein Conformation; D013401:Sugar Alcohol Dehydrogenases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D020124:Thermotoga maritima / Q000201:enzymology*
D013401:Sugar Alcohol Dehydrogenases; C020672:glycerol dehydrogenase