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  4. Characterization of the Thermobifida fusca Xylanase 11A Carbohydrate-Binding Module by X-ray Crystallography

Characterization of the Thermobifida fusca Xylanase 11A Carbohydrate-Binding Module by X-ray Crystallography

File(s)
Wolski, Paul - Research Honors Thesis.pdf (137.81 KB)
Permanent Link(s)
https://hdl.handle.net/1813/29613
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College of Agriculture and Life Sciences Honors Theses
Author
Wolski, Paul
Abstract

Xylanase 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.

Date Issued
2012-07-31
Type
dissertation or thesis

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