Author

S. Pospich

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Biochemistry· 4 Biophysics· 2

Signature Assays, Organisms & Methods

Click to filter · or open tag

Assay:cryo-EM· 5 Approach:experimental assay· 4 Research Focus:protein structure prediction· 3 Approach:deep learning· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Organism:human· 1

Frequent Co-Authors

S. Raunser· 6 shared T. Wagner· 3 shared M. Stabrin· 2 shared A. Belyy· 1 shared A. Houdusse· 1 shared A. L. Kho· 1 shared B. U. Klink· 1 shared C. Gatsogiannis· 1 shared

Activity by Year

2019-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

6 shared papersBiochemistry

S. Raunser

Mutual co-authors in cluster

Author profile →

6 papers

Recent·Most cited

Structural basis of actin filament assembly and aging

W. Oosterheert, B. U. Klink, A. Belyy, S. Pospich, S. Raunser

This study presents cryo-EM structures of F-actin in all nucleotide states, revealing how water molecules drive ATP hydrolysis and filament dynamics, and explains differences in polymerization rates between Ca2+ and Mg2+-actin.

bioRxiv · Mar 29, 2022Biochemistry

Structure of the thin filament in native skeletal muscles reveals its interaction with nebulin and two distinct conformations of myosin

Z. Wang, M. Grange, S. Pospich, T. Wagner, A. L. Kho, M. Gautel, S. Raunser

The paper presents the first structure of native nebulin bound to thin filaments in sarcomeres, revealing interactions with actin and myosin conformations, and the molecular basis of nebulin's role in muscle function.

bioRxiv · Oct 6, 2021 · PreprintBiochemistry

High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism

S. Pospich, L. Sweeney, A. Houdusse, S. Raunser

The paper reports high-resolution cryo-EM structures of actomyosin-V in three nucleotide states, revealing structural transitions and insights into force generation.

bioRxiv · Sep 7, 2021Biochemistry

TranSPHIRE: Automated and feedback-optimized on-the-fly processing for cryo-EM

M. Stabrin, F. Schoenfeld, T. Wagner, S. Pospich, C. Gatsogiannis, S. Raunser

TranSPHIRE automates cryo-EM data processing during acquisition, using a feedback loop to improve particle picking and produce high-resolution 3D reconstructions.

bioRxiv · Jun 16, 2020Biophysics

Two particle picking procedures for filamentous proteins: SPHIRE-crYOLO filament mode and SPHIRE-STRIPER

T. Wagner, L. Lusnig, S. Pospich, M. Stabrin, F. Schönfeld, S. Raunser

This paper introduces two methods for selecting filamentous proteins from cryo-EM images: a deep learning approach in SPHIRE-crYOLO and a line detection approach in SPHIRE-STRIPER, showing their performance on tobacco mosaic virus and F-actin datasets.

bioRxiv · Feb 28, 2020Biophysics

Structural effects and functional implications of phalloidin and jasplakinolide binding to actin filaments

S. Pospich, F. Merino, S. Raunser

This study examines how phalloidin and jasplakinolide affect actin filament structure and function by stabilizing different states during actin dynamics.

bioRxiv · Oct 5, 2019Biochemistry