Author

S. T. Huber

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· 3 Microbiology· 1

Signature Assays, Organisms & Methods

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Assay:cryo-EM· 4 Approach:experimental assay· 4 Organism:bacteria (other)· 2 Research Focus:cell signaling & trafficking· 2 Research Focus:protein folding & dynamics· 2 Research Focus:protein structure prediction· 2 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

A. J. Jakobi· 3 shared W. H. Evers· 2 shared B. Junglas· 1 shared C. de Agrela Pinto· 1 shared C. Sachse· 1 shared C. Taisne· 1 shared D. Mann· 1 shared D. Maresca· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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3 shared papersBiophysics

A. J. Jakobi

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Structural basis of membrane targeting and coatomer assembly by human GBP1

T. I. Kuhm, L. Gross, C. de Agrela Pinto, S. T. Huber, C. Taisne, E. A. Giannopoulou, E. Pardon, J. Steyaert, S. J. Tans, A. J. Jakobi

This study determines the cryo-EM structure of human GBP1 dimer and coatomer assemblies, revealing how nucleotide binding and hydrolysis drive membrane targeting and coatomer formation.

bioRxiv · Mar 28, 2023Biophysics

Cryo-EM structure of gas vesicles for buoyancy-controlled motility

S. T. Huber, D. Terwiel, W. H. Evers, D. Maresca, A. J. Jakobi

The paper determines the cryo-EM structure of gas vesicles from B. megaterium, revealing their self-assembly mechanism and structural features that enable buoyancy control.

bioRxiv · May 8, 2022Biophysics

Nanofluidic chips for cryo-EM structure determination from picoliter sample volumes

S. T. Huber, E. Sarajlic, R. Huijink, F. Weis, W. H. Evers, A. J. Jakobi

This paper introduces nanofluidic chips for cryo-EM that enable reproducible ice thickness from picoliter samples, improving high-resolution structure determination.

bioRxiv · May 25, 2021Biophysics

PspA adopts an ESCRT-III-like fold and remodels bacterial membranes

B. Junglas, S. T. Huber, T. Heidler, L. Schloesser, D. Mann, R. Hennig, M. Clarke, N. Hellmann, D. Schneider, C. Sachse

This study presents the cryo-EM structure of PspA and shows its ability to remodel bacterial membranes through ESCRT-III-like mechanisms.

bioRxiv · Sep 23, 2020Microbiology