Stefan Raunser

This study identifies two mechanisms controlling INF2 activity, showing how they limit actin remodeling and impact cellular processes and disease.

This paper introduces a streamlined workflow for montage cryo-electron tomography that simplifies data acquisition and processing, enabling high-throughput, nanoscale-resolution imaging of biological samples.

This paper develops and tests ideal efficacy photoswitch ligands for TRPC4/5 channels, enabling precise spatiotemporally-controlled modulation in live tissues.

The paper discovers that sarcomeres divide along the myofibril tension axis during Drosophila muscle development to add new sarcomeres while maintaining mechanical integrity.

This study investigates the multi-state kinetics of Tc toxin prepore-to-pore transition, identifying intermediate states and transition times under various conditions.

The paper presents a structural and functional analysis of the KMN network, revealing key interfaces and their role in stabilizing microtubule binding and force transmission during chromosome segregation.

The paper determines the structural assembly of yeast Oxalyl-CoA synthetase, revealing asymmetric hexameric arrangements and identifying key self-association interfaces.

This paper introduces a new cryogenic microscope that combines fluorescence, ion beam, and electron beam imaging to improve the targeting and fabrication of lamellae for high-resolution imaging.

The paper introduces hardware and software improvements to enhance cryo-FIB milling for cryo-electron tomography.

This paper determines the structure of the Lifeact-F-actin complex and shows how Lifeact competes with other actin-binding proteins, affecting cell morphology.

The paper reports cryo-EM structures of anthrax lethal toxin in its heptameric pre-pore state, revealing LF binding dynamics and conformational changes.

This study identifies two glycans, heparins/heparan sulfates and Lewis antigens, as receptors for Tc toxins, revealing a two-step adhesion mechanism involving glycan binding to toxin subunits.

The paper presents a high-resolution cryo-EM structure of a human BBSome core subcomplex, revealing its open conformation and interactions with cargo and membrane components.

The paper determines the structure of a Tc holotoxin pore and elucidates its translocation mechanism through conformational changes and lipid interactions.

The paper presents high-resolution structures of five TcA toxins from different bacteria, revealing conserved architecture and a common mechanism of action despite previous suggestions of variability.

This paper presents the first high-resolution cryo-EM structure of ClpXP from Listeria monocytogenes, revealing the binding interface and activation mechanism of the complex.

The paper reports the cryo-EM and crystal structures of XaxAB pore complex and monomers, revealing the mechanism of membrane insertion and function of Xax toxins.