CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF AN NAD+-DEPENDENT ALCOHOL-DEHYDROGENASE FROM THE EXTREME THERMOPHILIC ARCHAEBACTERIUM SULFOLOBUS-SOLFATARICUS(147 visite) PEARL L, DEMASI D, HEMMINGS A, SICA F, MAZZARELLA L, RAIA C, DAURIA S, ROSSI M
Parole chiave: Alcohol Dehydrogenase, Archaebacteria, Extreme Thermophile, Protein Thermostability, Sulfolobus Solfataricus, Nicotinamide Adenine Dinucleotide, Article, Crystal Structure, Nonhuman, Priority Journal, Protein Stability, Thermophilic Bacterium, X Ray Analysis, X-Ray Diffraction,
Biomol. Structure and Modelling Unit, Dept. of Biochem. and Molec. Biology, University College London, Gower Street, London WC1E 6BT, United Kingdom Dipartimento di Chimica, Univ. Studi di Napoli Federico II, Via Mezzocannone 4, 80134 Napoli, Italy Department of Crystallography, Birkbeck College, Malet Street, London WC1E 7HX, United Kingdom Ist. Biochim. Proteine Enzimologia, Consiglio Nazionale delle Ricerche, Via Marconi 12, I-80125 Napoli, Italy
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.
206 Records (200 escludendo Abstract e Conferenze). Impact factor totale: 808.208 (785.969 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 806.202 (782.565 escludendo Abstract e Conferenze).