Crystallization and preliminary X-ray analysis of an NAD+-dependent alcohol dehydrogenase from the extreme thermophilic archaebacterium Sulfolobus solfataricus

Pearl, Laurence H., Demasi, Domenico, Hemmings, Andrew M., Sica, Filomena, Mazzarella, Lelio, Raia, Carlo A., D'Auria, Sabato and Rossi, Mosè (1993) Crystallization and preliminary X-ray analysis of an NAD+-dependent alcohol dehydrogenase from the extreme thermophilic archaebacterium Sulfolobus solfataricus. Journal of Molecular Biology, 229 (3). pp. 782-784. ISSN 0022-2836

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Abstract

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 I4122 (a =126.82 Å, b = 118.95 Å) with a monomer in the asymmetric unit, and the single crystals diffract to 2.8 Å.

Item Type:	Article
Uncontrolled Keywords:	alcohol dehydrogenase,archaebacteria,extreme thermophile,protein thermostability,sulfolobus solfataricus,biophysics,structural biology,molecular biology ,/dk/atira/pure/subjectarea/asjc/1300/1304
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	LivePure Connector
Date Deposited:	13 Feb 2025 15:30
Last Modified:	16 Feb 2025 06:30
URI:	https://ueaeprints.uea.ac.uk/id/eprint/98469
DOI:	10.1006/jmbi.1993.1079

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