OIST-UT Joint talk series for future science-Season 3: "How close are we to atomic resolution cryo-electron microscopy of membrane proteins?"


Wednesday, March 17, 2021 - 17:30





How close are we to atomic resolution cryo-electron microscopy of membrane proteins?


Cryo-electron microscopy (cryo-EM) is rapidly gaining popularity as a powerful method for structural studies of biomolecules and their complexes. Over the last decade, the technique experienced a “revolution” in performance that was brought about by direct electron detector technologies and advanced image processing algorithms. Nowadays, cryo-EM routinely determines molecular structures with resolutions in the 2.5 – 3.5 Å range. Such results are adequate for modelling of the protein but lack fidelity for confident localization of water molecules and hydrogen atoms. Unambiguous elucidation of the biochemistry behind protein function and pharmacology of drugs would require atomic resolution structures, at levels below 1.5 Å. Last year, several groups worldwide, including us, demonstrated atomic resolution cryo-EM with a test sample comprising the “easy” soluble protein apoferritin. This was an important technological milestone showcasing the best-case-scenario capabilities of cryo-EM. However, membrane proteins, and other real-world samples, impose numerous experimental challenges, such as small size, heterogeneity, flexibility, preferential orientation, etc. Here, I will present our journey in pushing the performance boundaries of cryo-EM for challenging membrane proteins, and in particular, in our studies of the structure, pharmacology, and dynamics of G protein-coupled receptors.


Dr. Radostin Danev, Graduate School of Medicine, The University of Tokyo


Rado Danev studied physics at Sofia University in Bulgaria and received his Ph.D. at the National Institute for Physiological Sciences in Okazaki, Japan. In 2011, he became a group leader at the Max Planck Institute of Biochemistry in Munich, Germany, and in 2018 was appointed as a professor at the University of Tokyo, Japan. His group works on expanding the performance envelope of cryo-electron microscopy through the development of new approaches and quantitative investigation and optimization of various aspects of the experiment.


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