Author

C. Kupitz

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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Biophysics· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 3 Assay:structural biology· 2 Organism:bacteria (other)· 1 Assay:protein structure· 1 Approach:statistical model· 1

Frequent Co-Authors

M. S. Hunter· 3 shared A. Barty· 2 shared F. Poitevin· 2 shared M. Liang· 2 shared R. G. Sierra· 2 shared V. Mariani· 2 shared A. Batyuk· 1 shared A. Cohen· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 35 mutual co-author links

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3 shared papersBiophysics

M. S. Hunter

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3 papers

Recent·Most cited

Changes in an Enzyme Ensemble During Catalysis Observed by High Resolution XFEL Crystallography

N. Smith, M. Dasgupta, D. C. Wych, C. Dolamore, R. G. Sierra, S. Lisova, D. Marchany-Rivera, A. E. Cohen, S. Boutet, M. S. Hunter, C. Kupitz, F. Poitevin, F. R. Moss, A. S. Brewster, N. K. Sauter, , M. A. Wilson

The paper uses XFEL crystallography to observe conformational changes in an enzyme during catalysis, revealing ionization-linked dynamics that control catalytic activity.

bioRxiv · Aug 15, 2023Biochemistry

Cooperative Allostery and Structural Dynamics of Streptavidin at Cryogenic- and Ambient-temperature

E. Ayan, B. Yuksel, E. Destan, F. B. Ertem, G. Yildirim, M. Eren, O. M. Yefanov, A. Barty, A. Tolstikova, G. K. Ketawala, S. Botha, E. H. Dao, B. Hayes, M. Liang, M. H. Seaberg, , H. DeMirci

The paper presents two apo-streptavidin structures at different temperatures and reveals cooperative allostery through water-mediated interactions.

bioRxiv · Sep 23, 2021Biophysics

Enzyme Intermediates Captured "on-the-fly" by Mix-and-Inject Serial Crystallography

J. Olmos, S. Pandey, J. M. Martin-Garcia, G. Calvey, A. Katz, J. Knoska, C. Kupitz, M. S. Hunter, M. Liang, D. Oberthuer, O. Yefanov, M. Wiedorn, M. Heymann, M. Holl, K. Pande, , Our

This paper demonstrates a method to capture enzyme reactions in real-time using mix-and-inject serial crystallography, revealing antibiotic cleavage and kinetic transitions in Mycobacterium tuberculosis β-lactamase.

bioRxiv · Jan 18, 2018Biophysics