Crystallization and preliminary X-ray diffraction study of a xylanase from Trichoderma harzianum.
A 20,000 Mr xylanase from Trichoderma harzianum has been purified and crystallized from 20% (w/v) saturated ammonium sulphate solutions. The unit cell is orthorhombic, space group P2(1)2(1)2(1), with unit cell lengths a = 44.2 A, b = 94.1 A, c = 51.6 A. Data from native crystals and several potential heavy-atom derivatives have been collected. An X-ray analysis to at least 2.8 A resolution appears to be feasible.
Rose
D R
DR
Division of Biological Sciences, National Research Council Ottawa, Ontario, Canada.
Birnbaum
G I
GI
Tan
L U
LU
Saddler
J N
JN
D003460:Crystallization; D006026:Glycoside Hydrolases; D003904:Mitosporic Fungi / Q000201:enzymology*; D014242:Trichoderma / Q000201:enzymology*; D014961:X-Ray Diffraction; D043325:Xylan Endo-1,3-beta-Xylosidase
D006026:Glycoside Hydrolases; D043325:Xylan Endo-1,3-beta-Xylosidase