Crystallization and preliminary X-ray diffraction studies of the catalytic core of acetyl xylan esterase from Trichoderma reesei.
Acetyl xylan esterase is involved in the biodegradation of hemicellulose. It cleaves O-acetyl groups from xylan, which is the most abundant hemicellulose in nature. The catalytic core of acetyl xylan esterase from T. reesei has been crystallized and X-ray diffraction data at 2.3 A collected. The crystal belongs to the triclinic space group P1 with unit-cell parameters a = 50.3, b = 62. 1, c = 40.0 A, alpha = 110.1, beta = 113.6 and gamma = 97.9 degrees. The asymmetric unit contains two molecules.
Department of Chemistry, University of Joensuu, PO Box 111, 80101 Joensuu, Finland.
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Hakulinen
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Tenkanen
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Rouvinen
D000115:Acetylesterase / Q000737:chemistry*; D020134:Catalytic Domain; D003460:Crystallization; D015394:Molecular Structure; D008970:Molecular Weight; D014242:Trichoderma / Q000201:enzymology*; D014961:X-Ray Diffraction
D000115:Acetylesterase; C081851:acetylxylan esterase