Electron microscopy articles within Nature

Featured

  • Letter |

    This study reports the first application of Zernike phase contrast (ZPC) electron cryo-tomography to examine cellular processes without the need for labelling or sectioning; the technique is used to visualize the maturation of the cyanophage Syn5 inside its host cell, identifying subcellular compartments and five distinct Syn5 assembly intermediates.

    • Wei Dai
    • , Caroline Fu
    •  & Wah Chiu

  • Letter |

    The crystal structure of the complex formed by the B and C toxin complex proteins is reported, revealing how toxin complexes are processed and protected; the proteins assemble to form a large hollow structure that sequesters the cytotoxic portion of the C protein, and a β-propeller domain mediates attachment to the A protein in the native ABC complex.

    • Jason N. Busby
    • , Santosh Panjikar
    •  & J. Shaun Lott

  • Article |

    High-resolution cryo-EM density maps are used to present the structures of Drosophila and human 80S ribosomes in complex with eEF2, E-site transfer RNA and Stm1-like proteins, and reveal the presence of two additional structural layers in the ribosomes of metazoan eukaryotes.

    • Andreas M. Anger
    • , Jean-Paul Armache
    •  & Roland Beckmann

  • Article |

    The long-awaited structure of a telomerase holoenzyme, from Tetrahymena, has been obtained by electron microscopy; affinity labelling of subunits and modelling with NMR and crystal structures of various components allowed the identification of the catalytic core and subunit interactions, and the functional role of the subunits in telomerase processivity was enabled by performing the first reconstitution of the holoenzyme in vitro.

    • Jiansen Jiang
    • , Edward J. Miracco
    •  & Juli Feigon

  • Letter |

    The TcA component of Photorhabdus luminescens ABC-type toxin complexes forms a transmembrane pore and injects TcC, the functional component of the toxin, into the target cell by means of a syringe-like mechanism.

    • Christos Gatsogiannis
    • , Alexander E. Lang
    •  & Stefan Raunser

  • Article |

    Cryo-electron microscopy structures of key intermediates during the sequential assembly of the pre-initiation complex are presented; structures of the closed and open-promoter complexes allow insights into the process of promoter melting.

    • Yuan He
    • , Jie Fang
    •  & Eva Nogales

  • Letter |

    The structures of three distinct human transcription factor IID (TFIID) protein assemblies are solved using cryo-electron microscopy; by incorporating TAF8 and TAF10, the key structural changes that remodel TFIID during assembly are determined, particularly the transition from a symmetric core-TFIID to an asymmetric holo-complex.

    • Christoph Bieniossek
    • , Gabor Papai
    •  & Imre Berger

  • Letter |

    Stalled bacterial ribosomes can be rescued by interaction with SmpB protein and a highly structured transfer-messenger RNA, and a cryo-electron microscopy map of this complex now shows how EF-G-dependent translocation of this non-canonical ligand is facilitated by conformational changes in the ribosome and the transfer-messenger RNA.

    • David J. F. Ramrath
    • , Hiroshi Yamamoto
    •  & Christian M. T. Spahn

  • Letter |

    During translation, tRNAs enter the ribosome and then move sequentially through three sites, known as A, P and E, as they transfer their attached amino acids onto the growing peptide chain. How the ribosome facilitates tRNA translocation between the sites remains largely unknown. Now a study uses multiparticle cryoelectron microscopy of a ribosome bound to the translation elongation factor, EF-G, to get information about tRNA movement. It identifies two new substates and sees that translocation is linked to unratcheting of the 30S ribosomal subunit.

    • Andreas H. Ratje
    • , Justus Loerke
    •  & Christian M. T. Spahn

  • News |

    Spiralling electron beams have the potential to measure and manipulate the properties of single atoms.

    • Zeeya Merali

  • Article |

    During protein synthesis within the ribosome, transfer RNAs (tRNAs) move sequentially through different sites as their attached amino acids are transferred onto the growing protein chain. Large conformational movements accompany this process. Here, a staggering 1.9 million electron cryomicroscopy images of the ribosome have been processed to visualize these changes. The results reveal that the ribosome functions as a Brownian machine that couples spontaneous changes driven by thermal energy to directed movement.

    • Niels Fischer
    • , Andrey L. Konevega
    •  & Holger Stark

  • News & Views |

    Time-resolved electron microscopy can capture structural changes in active macromolecular complexes, but detailed imaging is essential. The dynamics of one step in protein synthesis has been deduced from two million images.

    • Måns Ehrenberg

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