Author

N. Nagaratnam

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· 3 Research Focus:protein folding & dynamics· 3 Organism:bacteria (other)· 2 Assay:protein structure· 2 Organism:human· 1 Assay:structural biology· 1

Frequent Co-Authors

J. M. Martin-Garcia· 3 shared P. Fromme· 3 shared R. Fromme· 2 shared A. Barty· 1 shared A. J. Flint· 1 shared A. Katz· 1 shared B. L. Nannenga· 1 shared C. Kupitz· 1 shared

Activity by Year

2018-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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3 shared papersBiochemistry

J. M. Martin-Garcia

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3 papers

Recent·Most cited

Structural and biophysical properties of FopA, a major outer membrane protein of Francisella tularensis

P. Fromme, N. Nagaratnam, J. M. Martin-Garcia, J.-H. Yang, M. R. Goode, G. Ketalawa, F. M. Craciunescu, J. D. Zook, T. D. Grant, R. Fromme, D. T. Hansen

This study determines the structural and biophysical properties of FopA, a major outer membrane protein of Francisella tularensis, revealing its dimeric, two-domain organization.

bioRxiv · Apr 8, 2022Biochemistry

New Structural Insights into the Function of the Catalytically Active Human Taspase1

N. Nagaratnam, S. Delker, R. Jernigan, T. E. Edwards, J. Snider, D. Thifault, D. Williams, B. L. Nannenga, M. Stofega, L. Sambucetti, J. Hsieh, A. J. Flint, P. Fromme, J. M. Martin-Garcia

This study determines the crystal structure of catalytically active human Taspase1 and identifies a long helical domain essential for its enzymatic activity, suggesting it as a potential target for anticancer therapeutics.

bioRxiv · Nov 26, 2020Biochemistry

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