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
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.