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Titolo:
Crystallization and preliminary X-ray diffraction analysis of the 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes
Autore:
Tsai, LC; Shyur, LF; Lin, SS; Yuan, HS;
Indirizzi:
Acad Sinica, Inst Mol Biol, Taipei, Taiwan Acad Sinica Taipei TaiwanAcad Sinica, Inst Mol Biol, Taipei, Taiwan Acad Sinica, Inst Bioagr Sci, Taipei, Taiwan Acad Sinica Taipei TaiwanAcad Sinica, Inst Bioagr Sci, Taipei, Taiwan
Titolo Testata:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
, volume: 57, anno: 2001,
parte:, 9
pagine: 1303 - 1306
SICI:
0907-4449(200109)57:<1303:CAPXDA>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
CRYSTAL-STRUCTURE; BETA-GLUCANASE; BACILLUS 1,3-1,4-BETA-GLUCANASE; BARLEY 1,3-1,4-BETA-GLUCANASE; MOLECULAR-CLONING; DNA-SEQUENCE; GENE; 4-GLUCANOHYDROLASE; LICHENIFORMIS; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Yuan, HS Acad Sinica, Inst Mol Biol, Taipei, Taiwan Acad Sinica Taipei Taiwan inica, Inst Mol Biol, Taipei, Taiwan
Citazione:
L.C. Tsai et al., "Crystallization and preliminary X-ray diffraction analysis of the 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes", ACT CRYST D, 57, 2001, pp. 1303-1306

Abstract

The truncated 1,3-1,4-beta -glucanase (1,3-1,4-beta -D-glucan 4-glucanohydrolase; E.C. 3.2.1.73) from Fibrobacter succinogenes was crystallized in four different forms by the vapour-diffusion method. Form A crystals have thelargest trigonal P321 unit cell, diffracting to 3.0 Angstrom resolution with four to six molecules per asymmetric unit. Form B and C crystals belong to the same monoclinic space group P2(1), but the form B unit cell is twiceas large as the unit cell of form C. Form B crystals diffract to 2.5 Angstrom resolution and contain four molecules per asymmetric unit. Form C crystals diffract to 2.1 Angstrom resolution and contain two molecules per asymmetric unit. Form D crystals have the smallest orthorhombic P2(1)2(1)2(1) unit cell, containing only one molecule per asymmetric unit, and diffract beyond 2.1 Angstrom resolution. The crystallization conditions for form B and C crystals are almost identical, except that form C crystals were grown in the presence of 2 mM Ca2+ ions. It is likely that Ca2+ directly binds to the glucanase, leading to unit-cell shrinkage as observed in other Bacillus glucanase crystals. A self-rotation search identified non-crystallographic twofold axes that combine with the crystallographic twofold dyads to give 222 symmetry for both form A and form B crystals, indicating that the glucanase has a tendency to pack in 222 symmetry.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/05/20 alle ore 14:38:04