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Titolo:
PURIFICATION, CRYSTALLIZATION AND PRELIMINARY-X-RAY CRYSTAL-STRUCTUREANALYSIS OF COPPER AMINE OXIDASE FROM ARTHROBACTER-GLOBOFORMIS
Autore:
FREEMAN HC; GUSS JM; KUMAR V; MCINTIRE WS; ZUBAK VM;
Indirizzi:
UNIV SYDNEY,SCH CHEM SYDNEY NSW 2006 AUSTRALIA UNIV SYDNEY,DEPT BIOCHEM SYDNEY NSW 2006 AUSTRALIA DEPT VET AFFAIRS MED CTR,DIV MOLEC BIOL SAN FRANCISCO CA 94121 UNIV CALIF SAN FRANCISCO,DEPT BIOCHEM & BIOPHYS SAN FRANCISCO CA 94143 UNIV CALIF SAN FRANCISCO,DEPT ANESTHESIA SAN FRANCISCO CA 94143
Titolo Testata:
Acta crystallographica. Section D, Biological crystallography
, volume: 52, anno: 1996,
parte:, 1
pagine: 197 - 198
SICI:
0907-4449(1996)52:<197:PCAPC>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
PIG PLASMA; IONS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
18
Recensione:
Indirizzi per estratti:
Citazione:
H.C. Freeman et al., "PURIFICATION, CRYSTALLIZATION AND PRELIMINARY-X-RAY CRYSTAL-STRUCTUREANALYSIS OF COPPER AMINE OXIDASE FROM ARTHROBACTER-GLOBOFORMIS", Acta crystallographica. Section D, Biological crystallography, 52, 1996, pp. 197-198

Abstract

beta-Phenylethylamine oxidase from the Gram-positive bacterium Arthrobacter globoformis has been crystallized as three crystal forms. Two belong to space group C2 and one to space group P2(1)2(1)2(1), respectively. The unit-cell volumes are consistent with one subunit of 70 644 Da per asymmetric unit for the two monoclinic forms, and with two subunits per asymmetric unit for the orthorhombic crystals. Three-dimensional intensity data have been recorded to 2.8 Angstrom resolution for one of the monoclinic crystal forms and to 3 Angstrom resolution for the orthorhombic crystal form.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 07:29:44