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Articles tagged "cryo-EM"

  • The 16th European Microscopy Congress 2016

    New developments in direct electron detecting cameras and their importance for cryo-EM.

    Richard Henderson (1)

    1. Structural Studies Division, MRC laboratory of Molecular Biology, Cambridge, Royaume Uni

    Direct electron detectors have played a key role in the recent increase in the power of single particle electron cryomicroscopy (cryo-EM). In this talk, I…
  • The 16th European Microscopy Congress 2016

    A versatile high-vacuum cryo transfer system for cryo microscopy and analytics

    Sebastian Tacke (1, 2), Vladislav Krzyzanek (3), Harald Nüsse (1), Alexander Rosenthal (4), Jürgen Klingauf (1), Roger Albert Wepf (5), Rudolf Reichelt (1)

    1. Institute of Medical Physics and Biophysics, University of Münster, Münster, Allemagne 2. Scientific Center for Optical and Electron Microscopy, ETH Zürich, Zürich, Suisse 3. Institute of Scientific Instruments of the CAS, The Czech Academy of Sciences, Brno, République tchèque 4. Microscopy Improvements e.U., Eisenstadt, Autriche 5. Centre for Microscopy & Microanalysis, University of Queensland, Brisbane, Autriche

    The conservation of the native state during sample preparation is mandatory for a correct interpretation of any micrograph. Particularly for EM, the preservation of the…
  • The 16th European Microscopy Congress 2016

    The interior of the rotavirus capsid

    Leandro F. Estrozi (1)

    1. Methods in electron microscopy (MEM), Institut de Biologie Structurale, Grenoble, France

    Rotavirus and other double-stranded RNA viruses confine and protect their genome inside the capsid even after cell entry, hiding viral ds-RNA from the cellular immune…
  • The 16th European Microscopy Congress 2016

    High resolution cryo-EM of eukaryotic proteasomes: an emerging tool for therapeutic drug development

    Paula da Fonseca (1)

    1. MRC Laboratory of Molecular Biology, -, Cambridge, Royaume Uni

    Recently the field of biological structural electron microscopy has seen an enormous transformation, primarily triggered by the availability of improved electron microscopes and direct electron…
  • The 16th European Microscopy Congress 2016

    Our muscle at near-atomic resolution – Cryo-EM structure of the F-actin-tropomyosin complex.

    Julian von der Ecken (1), Mirco Müller (2), William Lehman (3), Dietmar J. Manstein (2), Pawel A. Penczek (4), Stefan Raunser (1)

    1. Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Allemagne 2. Institute for Biophysical Chemistry, Hannover Medical School, Hannover, Allemagne 3. Department of Physiology and Biophysics, Boston University School of Medicine, Boston, Etats-Unis 4. Department of Biochemistry and Molecular Biology, Houston Medical School, Houston, Etats-Unis

    Muscular movement plays an essential role not only in our lives but also describes a fundamental mechanism of force production. Filamentous actin (F-actin) is the major…
  • The 16th European Microscopy Congress 2016

    Structure-function insights reveal the human ribosome as a cancer target for antibiotics

    Alexander Myasnikov (1, 2, 3), Kundhavai Natchiar (1, 2, 3), Marielle Nebout (4, 5), Isabelle Isabelle Hazemann (1, 2, 3), Véronique Imbert (4, 5), Heena Khatter (1, 2, 3), Jean-François Peyron (4, 5), Bruno Klaholz (1, 2, 3)

    1. Centre for Integrative Biology (CBI), Department of Integrated Structural Biology, IGBMC (Institute of Genetics and of Molecular and Cellular Biology), Illkirch, France 2. Centre National de la Recherche Scientifique, CNRS, UMR 7104, Illkirch, France 3. Institut National de la Santé et de la Recherche Médicale, INSERM, U964, Illkirch, France 4. Centre Méditerranéen de Médecine Moléculaire (C3M), INSERM, UMR 1065, Nice, France 5. UFR Médecine, Faculté de Médecine, Université de Nice-Sophia Antipolis, Nice, France

    Abstract Many antibiotics in clinical use target the bacterial ribosome by interfering with several mechanistic steps of the protein synthesis machinery. However, targeting the human…
  • The 16th European Microscopy Congress 2016

    Cryo-EM Structural characterization of the M. tuberculosis ESX-1 secreted virulence factor EspB

    Giancarlo Tria (1), Giancarlo Tria (1), Axel Siroy (1), Chen Delei (1), Nino Iakobachvili (1), Hirotoshi Furusho (1), Carmen López-Iglesias (1), Raimond B. G. Ravelli (1), Peter J. Peters (1)

    1. The Multimodal Molecular Imaging institute, Maastricht University, Universiteitssingel 50, 6229 ER, , Maastricht, Pays-Bas

    Mycobacterium tuberculosis (Mtb) is the top infectious disease killer worldwide. The threat posed by this bacterium is higher than ever, with the recent discovery of…
  • The 16th European Microscopy Congress 2016

    Fusion to a symmetric scaffold allows cryo-EM analysis of a small monomeric protein

    Francesca Coscia (1, 2), Leandro Estrozi (1), Fabienne Hans (1), Hélène Malet (1), Marjolaine Noirclerc-Savoye (1), Guy Schoehn (1), Carlo Petosa (1)

    1. Structural Biology Institute, CNRS/CEA/UGA, Grenoble, France
    2. Institute of Structural and Molecular Biology, Birkbeck College, London, Royaume Uni

    Single particle cryo-electron microscopy (cryoEM) is a powerful method for determining the structures of large macromolecules and their complexes. Recent technical advances in direct electron…
  • The 16th European Microscopy Congress 2016

    Structure of the bacterial type 3 secretion system in action

    Mikhail Kudryashev (1, 1, 2)

    1. Max Planck Institute for Biophysics, Frankfurt am Main, Allemagne 2. Buchmann Institute for Molecular Life Sciences, Goethe University of Frankfurt, Frankfurt am Main, Allemagne

    Pathogenic bacteria commonly use the conserved type 3 secretion system (T3SS or Injectisome) to deliver virulence factors into the target eukaryotic cells in order to…

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