Crystallization and preliminary X-ray analysis of an NAD(+)-dependent alcohol dehydrogenase from the extreme thermophilic archaebacterium Sulfolobus solfataricus.
An NAD(+)-dependent alcohol dehydrogenase from the extreme thermophilic archaebacterium Sulfolobus solfataricus has been crystallized in the holo-enzyme and apo-enzyme forms. Crystals of the holo-enzyme grow from 2-methyl-2,4-pentanediol at pH 8.4 with the addition of NADH and at pH 7.0 with the addition of NADH and dimethyl sulphoxide. Crystals of the apo-enzyme grow at pH 6.3 from a mixture of polyethylene glycol 4000 and propan-2-ol. The holo-enzyme crystallizes in C2 with a dimer in the asymmetric unit, however the crystals are twinned and unsuitable for data collection. The apo-enzyme crystallizes in I4(1)22 (a = 126.82 A, b = 118.95 A) with a monomer in the asymmetric unit, and the single crystals diffract to 2.8 A.
Pearl
L H
LH
Department of Biochemistry and Molecular Biology, University College London, U.K.
Demasi
D
D
Hemmings
A M
AM
Sica
F
F
Mazzarella
L
L
Raia
C A
CA
D'Auria
S
S
Rossi
M
M
D000426:Alcohol Dehydrogenase / Q000737:chemistry* / Q000378:metabolism; D009243:NAD / Q000378:metabolism*; D016944:Sulfolobus / Q000201:enzymology*; D014961:X-Ray Diffraction
D009243:NAD; D000426:Alcohol Dehydrogenase