Jan-Hannes Schäfer

This study determines the structural and mechanistic basis of FapB amyloid assembly in Pseudomonas, showing it forms cross-β-solenoid fibrils and interacts with FapC fibrils.

This study uses cryo-EM to reveal structural plasticity and ligand promiscuity of CYP3A4, showing multiple conformations and highlighting the F/G loop's role in binding pocket remodeling.

The paper identifies tailocins as contaminants in ex vivo amyloid preparations and proposes strategies to detect and avoid them in cryo-EM.

This study identifies two mechanisms by which dipeptide esters disrupt lysosomal homeostasis: amyloid fibril formation and proximity labeling via Cathepsin C.

This paper introduces DM, a detergent that reduces air-water interface artifacts in cryo-EM, improving reconstruction quality and particle stability.

The paper uses cryo-EM to study P-glycoprotein in different environments, revealing distinct roles of transmembrane helices 4 and 10 in its functional plasticity.

This study uses proteomics and 3D imaging to show that ATTR cardiac amyloidosis involves microangiopathy, capillary occlusion, and vascular basement membrane congestion.

This study determines the structure of TIRAP filaments and identifies the role of the N-terminal PBM in regulating their assembly and function at the plasma membrane.

CryoSift automates 2D class selection in cryo-EM by using a CNN to assess particle quality, enabling high-throughput processing for high-resolution reconstructions.

Magellon provides a flexible and scalable cryo-EM platform with microservices architecture for data management, processing, and visualization.

This study compares the structural and functional mechanisms of Mon1-Ccz1 and Fuzzy-Inturned RabGEFs to explain their target specificity and membrane recruitment.

This study systematically analyzes the conformational spectrum of the bacterial ABC transporter MsbA in twelve different membrane mimetics using cryo-EM, revealing environment-specific structural responses.

The paper determines the cryo-EM structure of the SPT-Orm2 complex and shows Orm2 has higher inhibitory potential than Orm1, despite similar structures.