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APR 29, 2021 9:00 AM PDT
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Cryo-Electron Microscopy: membrane proteins down to atoms

Speakers
  • Assistant Professor, Dept of Molecular & Cell Biology Helen Wills Neuroscience Institute, University of California, Berkeley
    Biography

      Dr. Stephen Brohawn is an Assistant Professor of Neurobiology at the University of California, Berkeley in the Department of Molecular and Cell Biology and the Helen Wills Neuroscience Institute. Research in the Brohawn laboratory is focused on understanding the basis of sensory transduction and electrical signaling in the nervous system. To this end, the lab uses cryo-electron microscopy as a major tool to investigate the structure and function of membrane protein ion channels and transporters. Dr. Brohawn is a New York Stem Cell Foundation - Robertson Neuroscience Investigator and his work has been recognized with a Sloan Research Fellowship, a McKnight Neuroscience Scholar Award, and a Klingenstein-Simons Research Fellowship. Prior to starting his laboratory in 2016, Dr. Brohawn was a Helen Hay Whitney Postdoctoral Fellow in Dr. Roderick MacKinnon's lab at the Rockefeller University from 2010 to 2015 where he studied ion channels that sense mechanical force. Steve received his PhD in Biology in 2010 from the Massachusetts Institute of Technology for his work with Dr. Thomas Schwartz on the structure and function of the nuclear pore complex. He received his B.S. from the University of Delaware in 2004 where he worked with Dr. Colin Thorpe on the enzymology of oxidative protein folding.

    • Senior Applications Development Scientist
      Biography

        Abhay received his PhD in Structural Biology at the University of Oxford, UK. He spent further time at Oxford as a post-doc continuing to a position as Senior Research Scientist. Abhay has been with Thermo Fisher Scientific for over two years and in expert in single particle analysis, MicroED and cryo-electron tomography.

      • Product Marketing Manager Life Sciences Business Unit, Materials and Structural Analysis, Analytical Instruments Group, Thermo Fisher Scientific
        Biography
          Marc Storms has studied biology / plant pathology at Wageningen University and UC Davis. He obtained his PhD in Virology studying the intercellular trafficking of Bunyaviruses. After his PhD he joined Philips / FEI Electron Optics / Thermo Fisher Scientific, first as applications specialist TEM and later as Product Manager where he has been involved in the (hardware and software) development and release of various Transmission Electron Microscopes (e.g. Morgagni and Tecnai Spirit) as well as instruments for sample preparation (Vitrobot Mk I-IV generations).
          Currently, Marc is responsible for the product marketing of Structural Biology related products and workflow solutions for single particle analysis (SPA). As such, he has been involved in new key initiatives for structural biology Cryo-EM solutions such as the Titan Krios, the Talos Arctica, Talos L120C, applications software developments for SPA (i.e. EPU SW) as well as methods to enhance contrast and detector performance such as the Volta phase plate and several generations of the Falcon direct electron detectors.

        Abstract

        Date:  April 29, 2021

        Time: 9:00am PST

         

        Cryo-electron microscopy (cryo-EM) reached single-atom resolution for 3D structure determination of biological macromolecules. Cryo-EM has been determining the structures of protein structures for soluble as well as membrane proteins that have a key role in human disease. It has become possible to obtain sufficiently high resolution structures to visualize water molecules, hydrogen atoms and in the cases of optimized samples, individual protein atoms. For protein structures, especially membrane proteins, improvements in resolution below 3 Å would mean improved rotamer assignments due to better defined side chain densities, visualization of bound drug or ligand molecules and an unambiguous assignment of structurally ordered water molecules that are very important for any structure-based drug discovery. The resolution leap is possible due to cryo-EM technological advances. We will review how our 300 kV, cryo-transmission electron microscope (Thermo Fisher Krios G4) works from the cold field emission source to detector and Selectris Imaging Filter. We will also show brand new results on membrane protein structures going beyond 2.5 Å resolution obtained with our 200kV Glacios cryo-TEM.

         

        Learning Objectives

        • Discover the implications of atomic resolution cryo-EM for structural biology
        • Explore recent research on membrane structures from both 200kV and 300kV cryo-TEM
        • Tour a cryo-EM microscope from cold field emission source, detectors and image/energy filtering

         

         

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