Cryoelectron microscopy

Cryoelectron microscopy is a method for imaging frozen-hydrated specimens at cryogenic temperatures by electron microscopy. Specimens remain in their native state without the need for dyes or fixatives, allowing the study of fine cellular structures, viruses and protein complexes at molecular resolution.

Latest Research and Reviews

  • Research | | open

    The biogenesis of eukaryotic ribosomes is a multi-step process involving the action of more than 200 different ribosome assembly factors. Here the authors show that Rps20 acts as a conduit to coordinate maturation steps across the head domain of the nascent small ribosomal subunit.

    • Valentin Mitterer
    • , Ramtin Shayan
    • , Sébastien Ferreira-Cerca
    • , Guillaume Murat
    • , Tanja Enne
    • , Dana Rinaldi
    • , Sarah Weigl
    • , Hajrija Omanic
    • , Pierre-Emmanuel Gleizes
    • , Dieter Kressler
    • , Celia Plisson-Chastang
    •  & Brigitte Pertschy
  • Research | | open

    NMR structure determination is challenging for proteins with a molecular weight above 30 kDa and atomic-resolution structure determination from cryo-EM data is currently not the rule. Here the authors describe an integrated structure determination approach that simultaneously uses NMR and EM data and allows them to determine the structure of the 468 kDa dodecameric aminopeptidase TET2 complex.

    • Diego F. Gauto
    • , Leandro F. Estrozi
    • , Charles D. Schwieters
    • , Gregory Effantin
    • , Pavel Macek
    • , Remy Sounier
    • , Astrid C. Sivertsen
    • , Elena Schmidt
    • , Rime Kerfah
    • , Guillaume Mas
    • , Jacques-Philippe Colletier
    • , Peter Güntert
    • , Adrien Favier
    • , Guy Schoehn
    • , Paul Schanda
    •  & Jerome Boisbouvier
  • Research | | open

    Thorsten Wagner et al. present SPHIRE-crYOLO, a particle picking software for selecting particles from digital micrographs in cryoEM data. After training, the method automatically recognizes particles with high recall and precision, simplifying data pre-processing.

    • Thorsten Wagner
    • , Felipe Merino
    • , Markus Stabrin
    • , Toshio Moriya
    • , Claudia Antoni
    • , Amir Apelbaum
    • , Philine Hagel
    • , Oleg Sitsel
    • , Tobias Raisch
    • , Daniel Prumbaum
    • , Dennis Quentin
    • , Daniel Roderer
    • , Sebastian Tacke
    • , Birte Siebolds
    • , Evelyn Schubert
    • , Tanvir R. Shaikh
    • , Pascal Lill
    • , Christos Gatsogiannis
    •  & Stefan Raunser
  • Research | | open

    During stress, protein synthesis is inhibited through phosphorylation of the initiation factor eIF2 on its alpha subunit and its interaction with eIF2B. Here the authors describe a structure of the yeast eIF2B in complex with its substrate - the GDP-bound phosphorylated eIF2, providing insights into how phosphorylation results in a tighter interaction with eIF2B.

    • Yuliya Gordiyenko
    • , José Luis Llácer
    •  & V. Ramakrishnan
  • Research | | open

    Epsilon toxin (Etx) is a potent pore forming toxin (PFT) produced by Clostridium perfringens. Here authors show the cryo-EM structure of the Etx pore assembled on the membrane of susceptible cells and shed light on pore formation and mutant phenotypes.

    • Christos G. Savva
    • , Alice R. Clark
    • , Claire E. Naylor
    • , Michel R. Popoff
    • , David S. Moss
    • , Ajit K. Basak
    • , Richard W. Titball
    •  & Monika Bokori-Brown

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