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Titolo:
CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC STUDY OF HUMAN CKSHS1 - A CELL-CYCLE REGULATORY PROTEIN
Autore:
ARVAI AS; BOURNE Y; WILLIAMS D; REED SI; TAINER JA;
Indirizzi:
SCRIPPS CLIN & RES INST,DEPT MOLEC BIOL,10666 N TORREY PINES RD LA JOLLA CA 92037 SCRIPPS CLIN & RES INST,DEPT MOLEC BIOL LA JOLLA CA 92037 FAC MED SECTEUR NORD MARSEILLE,CRISTALLOG & CRISTALLISAT MACROMOLEC BIOL LAB F-13916 MARSEILLE 20 FRANCE
Titolo Testata:
Proteins
fascicolo: 1, volume: 21, anno: 1995,
pagine: 70 - 73
SICI:
0887-3585(1995)21:1<70:CAPCSO>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Keywords:
CELL CYCLE PROTEIN; CRYSTALLIZATION; X-RAY DIFFRACTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
11
Recensione:
Indirizzi per estratti:
Citazione:
A.S. Arvai et al., "CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC STUDY OF HUMAN CKSHS1 - A CELL-CYCLE REGULATORY PROTEIN", Proteins, 21(1), 1995, pp. 70-73

Abstract

The cell cycle regulatory protein CksHs1 has been crystallized in a form suitable for X-ray studies. CksHs1 crystals were grown in the presence of vanadate, a phosphatase inhibitor, but were also obtained withphosphate or tungstate as a cofactor. They belong to the hexagonal space group P6(1)22 with unit cell dimensions: a = b = 94 Angstrom, c = 131,6 Angstrom, and gamma = 120 degrees. The crystals grown in the presence of vanadate diffract X-rays to at least 2.8 Angstrom. Molecular replacement results from the homologous human CksHs2 structure reveal that a dimer forms the crystal habit, giving the unusual V-m value of 4.4 Angstrom(3)/Da or a solvent content of 72%. (C) 1995 Wiley-Liss, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 00:08:54