Crystallization and preliminary X-ray analysis of two major xylanases from Trichoderma reesei.
Two major endoxylanases, endo-beta-1,4-xylanase I and II (molecular mass 19 kDa and 21 kDa) from the filamentous fungus Trichoderma reesei have been crystallized by using ammonium sulphate as the precipitating agent. Both crystals were monoclinic and belonged to the space groups C2 (a = 71.9 A, b = 39.0 A, c = 59.9 A, beta = 118.0 degrees, for XYNI) and P2(1) (a = 81.6 A, b = 60.6 A, c = 38.3 A, beta = 94.4, for XYNII). The crystals diffract to at least 2.2 A and 1.5 A, respectively.
Department of Chemistry, University of Joensuu, Finland.
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A
Törrönen
J
J
Rouvinen
M
M
Ahlgren
A
A
Harkki
K
K
Visuri
D003460:Crystallization; D043364:Endo-1,4-beta Xylanases; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000302:isolation & purification; D007527:Isoenzymes / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D013045:Species Specificity; D014242:Trichoderma / Q000201:enzymology*; D014961:X-Ray Diffraction / Q000379:methods
D007527:Isoenzymes; D006026:Glycoside Hydrolases; D043364:Endo-1,4-beta Xylanases