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Titolo:
CRYSTALLIZATION AND PRELIMINARY-X-RAY CRYSTALLOGRAPHIC STUDY OF RIBOSOME-INACTIVATING PROTEIN FROM BARLEY-SEEDS
Autore:
SONG HK; HWANG KY; KIM KK; SUH SW;
Indirizzi:
SEOUL NATL UNIV,COLL NAT SCI,DEPT CHEM SEOUL 151742 SOUTH KOREA SEOUL NATL UNIV,COLL NAT SCI,DEPT CHEM SEOUL 151742 SOUTH KOREA
Titolo Testata:
Acta crystallographica. Section D, Biological crystallography
, volume: 50, anno: 1994,
parte:, 6
pagine: 910 - 912
SICI:
0907-4449(1994)50:<910:CAPCSO>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
N-GLYCOSIDASE ACTIVITY; RICIN A-CHAIN; ANTIVIRAL PROTEIN; ANGSTROM; REPLICATION; INHIBITOR; DETECTOR; CELLS; SITE;
Tipo documento:
Note
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
36
Recensione:
Indirizzi per estratti:
Citazione:
H.K. Song et al., "CRYSTALLIZATION AND PRELIMINARY-X-RAY CRYSTALLOGRAPHIC STUDY OF RIBOSOME-INACTIVATING PROTEIN FROM BARLEY-SEEDS", Acta crystallographica. Section D, Biological crystallography, 50, 1994, pp. 910-912

Abstract

Ribosome-inactivating protein from barley seeds has been crystallizedusing polyethylene glycol as precipitant. The crystal belongs to the monoclinic space group C2, with unit-cell parameters a = 88.36, b = 62.59, c = 53.18 Angstrom and beta = 108.62 degrees. The asymmetric unitcontains one molecule of ribosome-inactivating protein with a corresponding crystal volume per protein mass (V-m) of 2.32 Angstrom(3) Da(-1) and a solvent content of 47% by volume. The crystal diffracts to about 2.3 Angstrom with X-rays from a rotating-anode source and is very stable in the X-ray beam. X-ray data (nearly complete to 2.4 Angstrom Bragg spacing) have been collected from a native crystal.

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Documento generato il 05/07/20 alle ore 13:14:51