J
Jesse A. Jones
Researcher at University of Tennessee Health Science Center
Publications - 10
Citations - 126
Jesse A. Jones is an academic researcher from University of Tennessee Health Science Center. The author has contributed to research in topics: Reductase & Topoisomerase. The author has an hindex of 4, co-authored 10 publications receiving 66 citations. Previous affiliations of Jesse A. Jones include Idaho State University & University of Michigan.
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Journal ArticleDOI
The structure of an iron-containing alcohol dehydrogenase from a hyperthermophilic archaeon in two chemical states
TL;DR: An iron-containing alcohol dehydrogenase from the hyperthermophilic archaeon Thermococcus thioreducens was crystallized in unit cells belonging to space groups P21, P212121 and P43212, and the crystal structures were solved at 2.4, 2.1 and 1.9 Å resolution by molecular replacement using the FeADH from Thermotoga maritima as a model.
Journal ArticleDOI
Small-Molecule Inhibition of the C. difficile FAS-II Enzyme, FabK, Results in Selective Activity.
Jesse A. Jones,Allan M. Prior,Ravi K. R. Marreddy,Rebecca D Wahrmund,Julian G Hurdle,Dianqing Sun,Kirk E. Hevener +6 more
TL;DR: In this article, the enoylacyl carrier protein (ACP) reductase II (FabK) was investigated as a potential drug target against C. difficile infection, which is a leading cause of significant morbidity, mortality and healthcare-related costs in the United States.
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Crystal structure of the 65-kilodalton amino-terminal fragment of DNA topoisomerase I from the gram-positive model organism Streptococcus mutans.
Jesse A. Jones,Kirk E. Hevener +1 more
TL;DR: The first structure of topoisomerase I is determined from the gram-positive bacterium, S. mutans, which displays a somewhat unique nine residue loop extension not present in any bacterial topoisomersase I structures previously determined other than that of an extremophile.
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A simplified protocol for high-yield expression and purification of bacterial topoisomerase I.
TL;DR: The systematic implementation and analysis of various expression and purification techniques leading to the development and optimization of a rapid and straightforward protocol for the auto-induced expression and two-step, affinity tag purification of Streptococcus mutans topoisomerase I yielding >20 mg/L of enzyme at over 95% purity.
Posted ContentDOI
Triggered reversible disassembly of an engineered protein nanocage
TL;DR: In this paper, a peptide capable of triggering conformational change at a key structural position in the largest known encapsulin nanocompartment is introduced, and the structure of the resulting engineered nanocage and demonstrate its ability to ondemand disassemble and reassemble under physiological conditions.