Crystals of family 11 xylanase II fromTrichoderma longibrachiatumthat diffract to atomic resolution
- 22 June 2004
- journal article
- research article
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section D-Biological Crystallography
- Vol. 60 (7) , 1275-1277
- https://doi.org/10.1107/s0907444904009400
Abstract
Xylanases catalyse the cleavage of various forms of xylan. A new crystal form of xylanase II from the fungus Trichoderma longibrachiatum that diffracts to better than 1 A resolution was grown from 12% PEG 8K, 0.1 M Tris pH 8.5, 0.2 M CaCl(2) with the addition of 2% glycerol to overcome crystal twinning. The crystals grow in a body-centered orthorhombic Bravais lattice, with unit-cell parameters a = 66.78, b = 67.94, c = 79.18 A. The solvent content is 42% with one molecule per asymmetric unit. Molecular-replacement analysis reveals the space group to be I222. This atomic resolution structure will provide important insights that will lead to a better understanding of the enzymatic mechanism of the family 11 xylanases.Keywords
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