Author

D. Beckett

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 2 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:bacteria (other)· 1 Research Focus:drug response / drug discovery· 1 Organism:human· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Approach:statistical model· 1

Frequent Co-Authors

A. D. MacKerell· 1 shared A. des Georges· 1 shared A. Diantonio· 1 shared A. Grishaev· 1 shared A. Krsitopeit· 1 shared A. Scudder· 1 shared A. Soares· 1 shared B. M. Roth· 1 shared

Activity by Year

2019-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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1 shared paperBiophysics

A. D. MacKerell

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

The structure of NAD+ consuming protein Acinetobacter baumannii TIR domain shows unique kinetics and conformations.

E. Klontz, J. O. Obi, Y. Wang, G. Glendening, J. Carr, C. Tsibouris, S. Buddula, S. Nallar, A. Soares, D. Beckett, J. S. Redzic, E. Eisenmesser, C. Palm, K. Schmidt, A. Scudder, , G. A. Snyder

The paper reports the crystal structure of Acinetobacter baumannii TIR domain and its NAD+ hydrolase activity, showing conformational changes and kinetic effects upon substrate binding.

bioRxiv · May 19, 2023 · PreprintBiochemistry

Unveiling the Catalytic Mechanism of GTP Hydrolysis in Microtubules

D. Beckett, G. A. Voth

This paper uses computational simulations to determine that a compacted microtubule lattice is necessary for GTP hydrolysis, with E254 as the catalytic residue, while an expanded lattice hinders hydrolysis.

bioRxiv · May 1, 2023Biochemistry

Structure of the cell-binding component of the Clostridium difficile binary toxin reveals a novel macromolecular assembly

X. Xu, R. Ruiz, K. A. Adipietro, C. Peralta, D. Ben-Hail, K. M. Varney, M. E. Cook, B. M. Roth, P. T. Wilder, T. Cleveland, A. Grishaev, H. Neu, S. Michel, W. Yu, D. Beckett, , D. J. Weber

This paper determines the atomic structures of the C. difficile binary toxin CDTb using cryoEM and X-ray crystallography, revealing novel di-heptamer forms and critical domains for toxicity and stability.

bioRxiv · Nov 10, 2019 · PreprintBiophysics