Purification, crystallization and preliminary X-ray study of beta-xylosidase from Trichoderma reesei

Citation
Am. Golubev et al., Purification, crystallization and preliminary X-ray study of beta-xylosidase from Trichoderma reesei, ACT CRYST D, 56, 2000, pp. 1058-1060
Citations number
16
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
56
Year of publication
2000
Part
8
Pages
1058 - 1060
Database
ISI
SICI code
0907-4449(200008)56:<1058:PCAPXS>2.0.ZU;2-C
Abstract
An extracellular multifunctional beta-xylosidase was purified from a cultur e of the fungus Trichoderma reesei. The active 95 +/- 5 kDa enzyme has been crystallized from sodium acetate buffer using PEG as a precipitant. The cr ystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 67.75, b = 98.54, c = 227.25 Angstrom, and diffract beyond 2.7 Angstrom resolution. X-ray data were collected from frozen crystals on a synchrotron source.