Dr Gonen is an expert in electron crystallography and cryo EM. He determined the 1.9Å resolution structure of the water channel aquaporin-0 by electron crystallography, the highest resolution for any protein determined by cryo EM techniques at the time. Dr Gonen established his own laboratory at the University of Washington in 2005 together with the very first cryo EM laboratory in the Pacific Northwest, a resource that continues to benefit many researchers at the UW School of Medicine and beyond. He has authored many publications from his laboratory concerning membrane protein structure and function. Dr Gonen was honored with a Career Development award from the American Diabetes Association as well as being chosen one of only 50 Howard Hughes Medical Institute Early Career Scientists around the country.

In 2011 Dr Gonen accepted a position as a Group Leader at the HHMI Janelia Research Campus where he began developing MicroED as a new method for structural biology. With this method Dr Gonen has pushed the boundaries of cryoEM and determined a number of previously unknown structures at resolutions close to 1Å. In 2012 he became a Member of the Royal Society of New Zealand and in a Professor of Biological Chemistry and Physiology at the David Geffen School of Medicine of the University of California, Los Angeles and an Investigator of the Howard Hughes Medical Institute.

Our laboratory studies the structures of membrane proteins important in homeostasis and signaling. We develop new tools in structural biology, namely MicroED as a new method for cryo EM, to facilitate the study of such membrane proteins to atomic resolution from vanishingly small crystals.

My laboratory studies the structures of membrane proteins that are important in maintaining homeostasis in the brain. Understanding structure, and hence function, requires scientists to build an atomic resolution map of every atom in the protein of interest, that is, an atomic structural model of the protein of interest captured in various functional states.

In 2013 we unveiled the method Microcrystal Electron Diffraction, MicroED, and demonstrated that it is feasible to determine high-resolution protein structures by electron crystallography of three-dimensional crystals in an electron cryo-microscope, CryoEM.

The CryoEM is used in diffraction mode for structural analysis of proteins of interest using vanishingly small crystals. The crystals are often a billion times smaller in volume than what is normally used for other structural biology methods like x-ray crystallography.

In this seminar I will describe the basics of this method, from concept to data collection, analysis and structure determination, and illustrate how samples that were previously unattainable can now be studied by MicroED. I will conclude by highlighting how this new method is helping us discover and design new drugs; shedding new light on chemical synthesis and small molecule chemistry; and showing us unprecedented level of details with important membrane proteins such as ion channels and G-protein coupled receptors, GPCRs, at atomic resolutions.