We use stain and cryo-electron microscopy (cryo-EM) and biochemical techniques to study the structure and function of membrane proteins and macromolecular complexes that play important roles in biology, human health, and disease.
Membrane proteins are involved in fundamental processes such as solute transport and signaling across the membrane. 70% of current drug targets are membrane proteins. To fully understand the function of a membrane protein, it is essential to know its structure. We use electron crystallography of two-dimensional (2D) crystals to determine the structure of membrane proteins in their near-to-native lipidic environment.
Besides structural studies we explore the function of membrane proteins by biochemical and electrophysiological studies. In most cellular processes proteins assemble in dynamic multi-protein assemblies. These complexes, however, are difficult to crystallize and it is therefore not fully understood how proteins assemble into macromolecular machines and how these machines perform their cellular functions.
We use single particle cryo electron microcopy (EM) to determine the structures of these complexes in order to elucidate their architecture and organization as well as to localize and interpret important protein-protein interactions.