49 Papers
214 Citations
Qi Xu is an academic researcher from National Renewable Energy Laboratory. The author has contributed to research in topics: Cellulase & Cellulosome. The author has an hindex of 23, co-authored 48 publications. Previous affiliations of Qi Xu include Oak Ridge National Laboratory & Tel Aviv University.
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Papers
A biophysical perspective on the cellulosome: new opportunities for biomass conversion.
Shi You Ding,Qi Xu,Michael F. Crowley,Yining Zeng,Mark R. Nimlos,Raphael Lamed,Edward A. Bayer,Michael E. Himmel +7 more
TL;DR: This review focuses on strategies likely to permit improved understanding of the bacterial cellulosome using biophysical approaches, with emphasis on advanced imaging and computational techniques.
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Versatile Derivatives of Carbohydrate-Binding Modules for Imaging of Complex Carbohydrates Approaching the Molecular Level of Resolution
Shi You Ding,Qi Xu,Mursheda K. Ali,John O. Baker,Edward A. Bayer,Yoav Barak,Raphael Lamed,Junji Sugiyama,Garry Rumbles,Michael E. Himmel +9 more
TL;DR: The distinct recognition properties of a double His-tagged recombinant CBM tagged with semiconductor quantum dots are employed for direct imaging of crystalline cellulose at the molecular level of resolution, using transmission and scanning transmission electron microscopy.
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Engineering enhanced cellobiohydrolase activity.
Larry E. Taylor,Brandon C. Knott,John O. Baker,P. Markus Alahuhta,Sarah E. Hobdey,Jeffrey G. Linger,Vladimir V. Lunin,Antonella Amore,Venkataramanan Subramanian,Kara Podkaminer,Qi Xu,Todd A. VanderWall,Logan A. Schuster,Yogesh B. Chaudhari,Yogesh B. Chaudhari,William S. Adney,Michael F. Crowley,Michael E. Himmel,Stephen R. Decker,Gregg T. Beckham +19 more
TL;DR: Compared CBHs from Trichoderma reesei and Penicillium funiculosum, which exhibit a multi-modular architecture consisting of catalytic domain (CD), carbohydrate-binding module, and linker, reveal CBH regions that enable targeted activity improvements.
Architecture of the Bacteroides cellulosolvens cellulosome: description of a cell surface-anchoring scaffoldin and a family 48 cellulase.
TL;DR: A large gene downstream of the primary Bacteroides cellulosolvens cellulosomal scaffoldin (cipBc, now renamed scaA), which contained an N-terminal leader peptide followed by 10 type I cohesins, an "X" domain of unknown structure and function, and a C- terminal S-layer homology (SLH) surface-anchoring module, was sequenced.
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In situ imaging of single carbohydrate-binding modules on cellulose microfibrils
D. J. Dagel,Yu San Liu,Lanlan Zhong,Yonghua Luo,Michael E. Himmel,Qi Xu,Yining Zeng,Shi You Ding,Steve Smith +8 more
TL;DR: Systematic orientations were observed that are consistent with the CBMs binding to the two opposite hydrophobic faces of the cellulose microfibril, with a well-defined orientation relative to the fiber axis, thus supporting a binding mechanism driven by chemical and structural recognition ofThe cellulose surface.
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