Author

U. J. Lorenz

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· 3 Biophysics· 1

Signature Assays, Organisms & Methods

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Assay:cryo-EM· 4 Approach:microscopy & imaging analysis· 3 Research Focus:protein structure prediction· 2 Approach:experimental assay· 1 Research Focus:protein folding & dynamics· 1 Organism:virus· 1

Frequent Co-Authors

M. Drabbels· 4 shared O. F. Harder· 4 shared G. Bongiovanni· 2 shared J. M. Voss· 2 shared P. K. Olshin· 1 shared S. V. Barrass· 1 shared

Activity by Year

2022-2023 · peak 2/yr

Co-Author Collaboration Network

6 top collaborators · 11 mutual co-author links

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4 shared papersBiochemistry

M. Drabbels

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4 papers

Recent·Most cited

Fast viral dynamics revealed by Microsecond Time-Resolved Cryo-EM

O. F. Harder, S. V. Barrass, M. Drabbels, U. J. Lorenz

This study uses microsecond time-resolved cryo-EM to observe fast protein dynamics in the cowpea chlorotic mottle virus capsid, revealing how pH changes trigger structural changes on the microsecond timescale.

bioRxiv · Apr 19, 2023Biochemistry

Near-atomic resolution reconstructions from in situ revitrified cryo samples

G. Bongiovanni, O. F. Harder, J. M. Voss, M. Drabbels, U. J. Lorenz

The paper demonstrates that near-atomic resolution cryo-EM reconstructions can be achieved from in situ revitrified samples, with homogeneous particle orientation.

bioRxiv · Feb 20, 2023 · PreprintBiochemistry

Microsecond melting and revitrification of cryo samples with a correlative light-electron microscopy approach

G. Bongiovanni, O. F. Harder, M. Drabbels, U. J. Lorenz

The paper introduces a method to capture microsecond dynamics of cryo samples using correlative light-electron microscopy with an optical microscope.

bioRxiv · Sep 14, 2022Biochemistry

Microsecond Melting and Revitrification of Cryo Samples - Protein Structure and Beam-Induced Motion

O. F. Harder, J. M. Voss, P. K. Olshin, M. Drabbels, U. J. Lorenz

This paper introduces a method to study protein dynamics in cryo-EM by melting and rapidly revitrifying samples, showing preserved structure and comparable beam-induced motion.

bioRxiv · Feb 14, 2022Biophysics