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Titolo:
CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF GLUCOSE-FRUCTOSE OXIDOREDUCTASE FROM ZYMOMONAS-MOBILIS
Autore:
LOOS H; ERMLER U; SPRENGER GA; SAHM H;
Indirizzi:
MAX PLANCK INST BIOPHYS,HEINRICH HOFFMANN STR 7 D-60528 FRANKFURT GERMANY MAX PLANCK INST BIOPHYS D-60528 FRANKFURT GERMANY KFA JULICH GMBH,FORSCHUNGSZENTRUM,INST BIOTECHNOL 1 D-52425 JULICH GERMANY
Titolo Testata:
Protein science
fascicolo: 12, volume: 3, anno: 1994,
pagine: 2447 - 2449
SICI:
0961-8368(1994)3:12<2447:CAPAOG>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
SORBITOL PRODUCTION; LOCALIZATION; ENZYME;
Keywords:
CRYSTALLIZATION; GLUCOSE-FRUCTOSE OXIDOREDUCTASE; NADP(H) COFACTOR; X-RAY CRYSTALLOGRAPHY; ZYMOMONAS MOBILIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
18
Recensione:
Indirizzi per estratti:
Citazione:
H. Loos et al., "CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF GLUCOSE-FRUCTOSE OXIDOREDUCTASE FROM ZYMOMONAS-MOBILIS", Protein science, 3(12), 1994, pp. 2447-2449

Abstract

Glucose-fructose oxidoreductase (E.C.1.1.99.-) from the ethanol-producing Gram-negative bacterium Zymomonas mobilis is a periplasmic, soluble enzyme that forms a homotetramer of 160 kDa with one NADP(H) cofactor per subunit that is tightly, but noncovalently, bound. The enzyme was crystallized by the hanging drop vapor diffusion method using sodium citrate as precipitant. The obtained crystals belong to the space group P2(1)2(1)2, with unit cell constants of 84.6 Angstrom, 94.1 Angstrom, and 117.0 Angstrom, consistent with two monomers in the asymmetricunit. They diffract to a resolution of about 2 Angstrom and are suitable for X-ray structure determination.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 05:20:06