Purification, crystallization and preliminary X-ray study of beta-xylosidase from Trichoderma reesei.
An extracellular multifunctional beta-xylosidase was purified from a culture of the fungus Trichoderma reesei. The active 95 +/- 5 kDa enzyme has been crystallized from sodium acetate buffer using PEG as a precipitant. The crystals 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 A, and diffract beyond 2.7 A resolution. X-ray data were collected from frozen crystals on a synchrotron source.
Golubev
A M
AM
Petersburg Nuclear Physics Institute, Gatchina, St Petersburg 188350, Russia.
Brandão Neto
J R
JR
Eneyskaya
E V
EV
Kulminskaya
A V
AV
Kerzhner
M A
MA
Neustroev
K N
KN
Polikarpov
I
I
D003460:Crystallization; D018360:Crystallography, X-Ray; D008970:Molecular Weight; D014242:Trichoderma / Q000201:enzymology*; D014995:Xylosidases / Q000737:chemistry* / Q000302:isolation & purification
D014995:Xylosidases; C026579:exo-1,4-beta-D-xylosidase