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• W2058497611 abstract "Xylanase II from Trichoderma reesei catalyzes the hydrolysis of glycosidic bonds in xylan. Crystallographic studies of this commercially important enzyme have been initiated to investigate its reaction mechanism, substrate binding and dependence on basic pH conditions. The wild-type protein was heterologously expressed in an Escherichia coli host using the defined medium and four active-site amino acids were replaced to abolish its activity (E177Q and E86Q) or to change its pH optimum (N44D and N44H). Cation-exchange and size-exclusion chromatography were used to obtain >90% protein purity. The ligand-free proteins and variant complexes containing substrate (xylohexaose) or product (xylotriose) were crystallized in several different space groups and diffracted to high resolutions (from 1.07 to 1.55 Å)." @default.
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• W2058497611 date "2013-02-27" @default.
• W2058497611 modified "2023-09-23" @default.
• W2058497611 title "Heterologous expression, purification, crystallization and preliminary X-ray analysis of<i>Trichoderma reesei</i>xylanase II and four variants" @default.
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• W2058497611 doi "https://doi.org/10.1107/s1744309113001164" @default.
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