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dc.contributor.authorWolski, Paul
dc.date.accessioned2012-07-31T19:36:30Z
dc.date.available2012-07-31T19:36:30Z
dc.date.issued2012-07-31
dc.identifier.urihttps://hdl.handle.net/1813/29613
dc.description.abstractXylanase 11A is an enzyme that degrades xylan. It was isolated from Thermobifida fusca, a thermophilic bacterium found in compost. Xyl11A also contains a family IIb carbohydrate-binding module (CMB), which has been found to be capable of binding to both cellulose and xylan, unlike some other family IIb CBMs. For this reason, this binding domain was chosen for characterization by X-ray crystallography. The gene for this binding domain was cloned into Escherichia coli and purified with column chromatography. Crystals were found in some crystallization screens, and diffraction of these crystals is currently pending.en_US
dc.language.isoen_USen_US
dc.titleCharacterization of the Thermobifida fusca Xylanase 11A Carbohydrate-Binding Module by X-ray Crystallographyen_US
dc.typedissertation or thesisen_US


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