Cryo-EM of infection-relevant protein complexes

Cryogenic electron microscopy of protein complexes relevant for bacterial infection

Cryogenic electron microscopy (Cryo-EM) has fundamentally changed structural biology in the last ten years and enables the determination of structures of heterogeneous proteins, large multiprotein complexes and membrane proteins in lipid environment. Therefore, the methodology was awarded with the Nobel Prize in Chemistry in 2017 (J. Dubochet, J. Frank, R. Henderson).
In the Roderer lab, we apply cryo-EM and single particle analysis to understand the structure-function relationship of: 

  • receptor-adhesin complexes

  • bacterial toxins

  • transmembrane receptors in lipid environment

In addition, we thrive to understand the molecular basis of microbial adhesion to the intestinal epithel of the host by cryogenic electron tomography (Cryo-ET).