title: Purification, crystallization and preliminary X-ray study of beta-xylosidase from Trichoderma reesei.
abstract: 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.
authors.affiliation: Petersburg Nuclear Physics Institute, Gatchina, St Petersburg 188350, Russia.
authors.forename: A M
authors.initials: AM
authors.lastname: Golubev
authors.forename: J R
authors.initials: JR
authors.lastname: Brandão Neto
authors.forename: E V
authors.initials: EV
authors.lastname: Eneyskaya
authors.forename: A V
authors.initials: AV
authors.lastname: Kulminskaya
authors.forename: M A
authors.initials: MA
authors.lastname: Kerzhner
authors.forename: K N
authors.initials: KN
authors.lastname: Neustroev
authors.forename: I
authors.initials: I
authors.lastname: Polikarpov
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D008970:Molecular Weight; D014242:Trichoderma / Q000201:enzymology*; D014995:Xylosidases / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: D014995:Xylosidases; C026579:exo-1,4-beta-D-xylosidase