Skip to main content


eCommons@Cornell >
Undergraduate Honors Theses >
College of Agriculture and Life Sciences Honors Theses >

Please use this identifier to cite or link to this item:
Title: Characterization of the Thermobifida fusca Xylanase 11A Carbohydrate-Binding Module by X-ray Crystallography
Authors: Wolski, Paul
Issue Date: 31-Jul-2012
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.
Appears in Collections:College of Agriculture and Life Sciences Honors Theses

Files in This Item:

File Description SizeFormat
Wolski, Paul - Research Honors Thesis.pdf137.81 kBAdobe PDFView/Open

Refworks Export

Items in eCommons are protected by copyright, with all rights reserved, unless otherwise indicated.


© 2014 Cornell University Library Contact Us