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Combining X-ray and Cryo-EM to study large and dynamic macromolecular complexes

10th Edition of International Conference on Structural Biology
March 15-16 2018 Barcelona, Spain

Holger Stark

Max-Planck Institute for Biophysical Chemistry, Germany

Keynote: Biochem Mol biol J

Abstract:

Single particle cryogenic electron microscopy (Cryo-EM) has developed into a powerful technique to determine 3D structures of large macromolecular complexes. Due to improvements in instrumentation and computational image analysis, the number of high-resolution structures is steadily increasing. The method can not only be used to determine high-resolution structures but also to study the dynamic behavior of macromolecular complexes and thus represents a very complementary method to X-ray crystallography. We have recently determined the structure of human proteasomes and their inhibition by anti-cancer drugs using X-ray crystallography to visualize the chemistry of inhibition at an unprecedented resolution of 1.8 Ã?Â?. By Cryo-EM, we were able to visualize the long-range allosteric conformational changes induced by the drug binding and visualized the effects of drug binding in terms of restrictions in the free-energy landscape of the human 26S proteasome. More examples of Cryo-EM studies of dynamic processes in large macromolecular complexes will be presented at the conference.

Biography :

Holger Stark has studied Biochemistry and completed his PhD from the Free University of Berlin, Germany. After a short Post-doctoral study at the Imperial College London (UK), he became a Group Leader at the University of Marburg (Germany) and moved from there to the Max-Planck-Institute in Göttingen (Germany) where he later became the Director in 2015. He has over 100 publications and an H-index of 45.
Email:hstark1@gwdg.de