Author

P. L. Xavier

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 structure prediction· 2 Assay:structural biology· 2 Research Focus:drug response / drug discovery· 1 Organism:E. coli· 1 Research Focus:host-pathogen & immune response· 1 Assay:imaging· 1

Frequent Co-Authors

L. Gelisio· 3 shared A. P. Mancuso· 2 shared H. N. Chapman· 2 shared J. Bielecki· 2 shared J. Knoska· 2 shared K. Lorenzen· 2 shared M. Galchenkova· 2 shared O. Yefanov· 2 shared

Activity by Year

2020-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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3 shared papersBiophysics

L. Gelisio

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Observation of a single protein by ultrafast X-ray diffraction

T. Ekeberg, D. Assalauova, J. Bielecki, R. Boll, B. J. Daurer, L. A. Eichacker, L. E. Franken, D. E. Galli, L. Gelisio, L. Gumprecht, L. H. Gunn, J. Hajdu, R. Hartmann, D. Hasse, A. Ignatenko, , F. R Maia

The paper demonstrates the first X-ray diffraction pattern from a single protein, Escherichia coli GroEL, showing the feasibility of ultrafast imaging of single proteins.

Light: Science & Applications · Jan 12, 2024Peer-reviewedBiophysics

Structure of the Lysinibacillus sphaericus Tpp49Aa1 pesticidal protein elucidated from natural crystals using MHz-SFX

L. J. Williamson, M. Galchenkova, H. L. Best, R. J. Bean, A. Munke, S. Awel, G. Pena, J. Knoska, R. Schubert, K. Doerner, H.-W. Park, D. K. Bideshi, A. Henkel, V. Kremling, B. Klopprogge, , D. Oberthur

This paper determines the structure of Tpp49Aa1 using MHz-SFX and investigates its interaction with Cry48Aa1, expanding its known target range to include additional mosquito species.

bioRxiv · Jan 14, 2022 · PreprintBiochemistry

Catalytic cleavage of HEAT and subsequent covalent binding of the tetralone moiety by the SARS-CoV-2 main protease

S. Günther, P. Y. A. Reinke, D. Oberthuer, O. Yefanov, H. Ginn, S. Meier, T. J. Lane, K. Lorenzen, L. Gelisio, W. Brehm, I. Dunkel, M. Domaracky, S. Saouane, J. Lieske, C. Ehrt, , G

The paper presents the crystal structure of SARS-CoV-2 main protease covalently bound to a metabolite of HEAT, revealing a pro-drug mechanism and potential for non-peptidic inhibitors.

bioRxiv · May 2, 2020 · PreprintBiophysics