Pearl L H, Demasi D, Hemmings A M, Sica F, Mazzarella L, Raia C A, D'Auria S, Rossi M
Department of Biochemistry and Molecular Biology, University College London, U.K.
J Mol Biol. 1993 Feb 5;229(3):782-4. doi: 10.1006/jmbi.1993.1079.
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.
