Christoph Gerle had his first contact with the structural studies of energy converting membrane complexes while working on the 2D crystallization of higher plant photosystem II in the laboratory of James Barber at the Imperial College, U.K. After moving to Kyoto University, Japan on a MEXT and JSPS fellowship to join the laboratory of Yoshinori Fujiyoshi for his graduate and postgraduate studies, he applied electron crystallography to study the structure of the bacterial V-ATPase from Thermus thermophilus leading to the discovery of the first dodecameric rotor ring in a rotary ATPase. As an assistant professor at the Career Path Unit of Kyoto University he started to challenge the structural analysis of the cell's most central energy converter: the intact mitochondrial F-ATP synthase. For this he is employing the full range of molecular electron microscopic techniques ranging from electron crystallography of two-dimensional crystals, over single-particle cryo-EM to electron cryo-tomography. The recent success to produce highly stable crystalline tubes of intact mitochondrial F-ATP synthase from bovine heart muscle made it possible to use cryo-EM for the elucidation of the F-ATP synthase's oligomeric structure and involvement in membrane curvature in an in vitro system for the first time.
Abstracts this author is presenting: