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Titolo:
The MinD protein from the hyperthermophilic archaeon Pyrococcus horikoshii: crystallization and preliminary X-ray analysis
Autore:
Sakai, N; Itou, H; Watanabe, N; Yao, M; Tanaka, I;
Indirizzi:
Hokkaido Univ, Grad Sch Sci, Div Biol Sci, Sapporo, Hokkaido 0600810, Japan Hokkaido Univ Sapporo Hokkaido Japan 0600810 oro, Hokkaido 0600810, Japan
Titolo Testata:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
, volume: 57, anno: 2001,
parte:, 6
pagine: 896 - 897
SICI:
0907-4449(200106)57:<896:TMPFTH>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
DIVISION INHIBITOR MINC; BACTERIAL-CELL DIVISION; TO-POLE OSCILLATION; ESCHERICHIA-COLI; RAPID POLE; FTSZ; PLACEMENT; SEPTUM; SITE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
16
Recensione:
Indirizzi per estratti:
Indirizzo: Watanabe, N Hokkaido Univ, Grad Sch Sci, Div Biol Sci, Sapporo, Hokkaido 0600810, Japan Hokkaido Univ Sapporo Hokkaido Japan 0600810 o 0600810, Japan
Citazione:
N. Sakai et al., "The MinD protein from the hyperthermophilic archaeon Pyrococcus horikoshii: crystallization and preliminary X-ray analysis", ACT CRYST D, 57, 2001, pp. 896-897

Abstract

MinD is one of the proteins regulating cell division. MinD from Escherichia coli has been designated as a type of motor protein which has an ATPase activity. This paper deals with the first crystallization and preliminary crystallographic analysis of recombinant MinD from Pyrococcus horikoshii (molecular weight 26.3 kDa) expressed in E. coli. Crystals of MinD were obtained by the hanging-drop vapour-iffusion method. MinD crystals belong to spacegroup P2(1)3, with unit-cell parameters a = b = c = 98.5 Angstrom, and diffract to 3.0 Angstrom resolution. The asymmetric units each contain one molecule of MinD, giving a crystal volume per protein mass (VM) of 3.0 Angstrom (3) Da(-1) and a solvent content of 59.0%.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/08/20 alle ore 20:35:22