Cryoelectron microscopy articles within Nature

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  • Article |

    Single-particle cryo-electron microscopy is used to resolve the structure of the phycobilisome, a 16.8-megadalton light-harvesting megacomplex, from the red alga Griffithsia pacifica at a resolution of 3.5 Å.

    • Jun Zhang
    • , Jianfei Ma
    •  & Sen-Fang Sui

  • Letter |

    The structure of mouse transient receptor potential mucolipin 1 (TRPML1), a cation channel located within endosomal and lysosomal membranes, is resolved using single-particle electron cryo-microscopy.

    • Qingfeng Chen
    • , Ji She
    •  & Youxing Jiang

  • Letter |

    The cryo-electron microscopy structure of the ten-subunit human transcription factor IIH, revealing the molecular architecture of the TFIIH core complex, the detailed structures of its constituent XPB and XPD ATPases, and how the core and kinase subcomplexes of TFIIH are connected.

    • Basil J. Greber
    • , Thi Hoang Duong Nguyen
    •  & Eva Nogales

  • Article |

    The structures of AMPA receptors in complex with auxiliary proteins are resolved by cryo-electron microscopy, and reveal conformational and permeation pathway changes that are associated with activation and desensitization of ionotropic glutamate receptors.

    • Edward C. Twomey
    • , Maria V. Yelshanskaya
    •  & Alexander I. Sobolevsky

  • Letter |

    New high-resolution cryo-electron microscopy structures of the HIV-1 envelope protein provide a detailed description and understanding of how the HIV-1 fusion machinery functions and how it changes its structure over time to convert from the pre-fusion to the fusion-intermediate conformation.

    • Gabriel Ozorowski
    • , Jesper Pallesen
    •  & Andrew B. Ward

  • Letter |

    Single-particle electron cryo-microscopy analysis of the mechanotransduction channel NOMPC reveals that it contains a bundle of four helical spring-shaped ankyrin repeat domains that undergo motion, potentially allowing mechanical movement of the cytoskeleton to be coupled to the opening of the channel.

    • Peng Jin
    • , David Bulkley
    •  & Yifan Cheng

  • Article |

    The structure of human ABCG2 bound to an inhibitory antibody using cryo-electron microscopy, representing the first high-resolution structural data of a human multidrug transporter.

    • Nicholas M. I. Taylor
    • , Ioannis Manolaridis
    •  & Kaspar P. Locher

  • Article |

    Structural ensembles of the 70S ribosome bound to cognate or near-cognate charged tRNAs in complex with EF-Tu illustrate the crucial role of the nucleotide G530 in decoding of mRNA, and demonstrate that translational fidelity results from direct control of GTPase by the decoding centre.

    • Anna B. Loveland
    • , Gabriel Demo
    •  & Andrei A. Korostelev

  • Article |

    The cryo-electron microscopy structure of the yeast spliceosome in a pre-catalytic state provides insights into the molecular events leading to formation of the spliceosome active site.

    • Clemens Plaschka
    • , Pei-Chun Lin
    •  & Kiyoshi Nagai

  • Article |

    Cryo-electron microscopy maps of the fission yeast Mediator complex and of a Mediator–RNA polymerase II holoenzyme reveal how changes in the Med14 subunit enable large-scale rearrangements of the Mediator structure that are essential for holoenzyme formation.

    • Kuang-Lei Tsai
    • , Xiaodi Yu
    •  & Francisco J. Asturias

  • Article |

    The first high-resolution (3.5 Å) structure of a full-length cyclic-nucleotide-gated channel, revealing an unconventional, voltage-insensitive voltage-sensor domain and a unique coupling mechanism between cyclic-nucleotide-binding and pore-opening.

    • Minghui Li
    • , Xiaoyuan Zhou
    •  & Jian Yang

  • Letter |

    The cryo-electron microscopy structure of a yeast spliceosome stalled before mature RNA formation provides insight into the mechanism of exon ligation.

    • Sebastian M. Fica
    • , Chris Oubridge
    •  & Kiyoshi Nagai

  • Article |

    Some CLC proteins are channels that conduct chloride ions passively, whereas others are active co-transporters, a difference that has been hard to understand given their high degree of sequence homology; now, cryo-electron microscopy is used to determine the structure of a mammalian CLC channel, shedding light on this question.

    • Eunyong Park
    • , Ernest B. Campbell
    •  & Roderick MacKinnon

  • Article |

    Two complementary studies present the full-length high-resolution structure of a Slo1 channel in the presence or absence of Ca2+ ions, in which an unconventional allosteric voltage-sensing mechanism regulates the Ca2+ sensor in addition to the voltage sensor’s direct action on the pore.

    • Xiao Tao
    • , Richard K. Hite
    •  & Roderick MacKinnon

  • Article |

    Two complementary studies present the full-length high-resolution structure of a Slo1 channel in the presence or absence of Ca2+ ions, in which an unconventional allosteric voltage-sensing mechanism regulates the Ca2+ sensor in addition to the voltage sensor’s direct action on the pore.

    • Richard K. Hite
    • , Xiao Tao
    •  & Roderick MacKinnon

  • Letter |

    The structure of the bacterial 70S ribosome in complex with ArfA, the release factor RF2, a short non-stop mRNA and a cognate P-site tRNA is presented, revealing how ArfA and RF2 facilitate alternative translation termination of the non-stop ribosomal complex using a stop-codon surrogate mechanism.

    • Chengying Ma
    • , Daisuke Kurita
    •  & Ning Gao

  • Article |

    The structures of several states on the pathway of SelB-mediated delivery of selenocysteine-specific tRNA to the ribosome in Escherichia coli reveal the mechanism of UGA stop codon recoding to selenocysteine and show how codon recognition triggers activation of translational GTPases.

    • Niels Fischer
    • , Piotr Neumann
    •  & Holger Stark

  • Letter |

    Structures of budding yeast RNA polymerase I in a catalytically active conformation are presented and confirmed by visualizing processive transcription along ribosomal DNA genes; they support a general model for transcription elongation in which contracted and expanded polymerase conformations are associated with active and inactive states, respectively.

    • Simon Neyer
    • , Michael Kunz
    •  & Achilleas S. Frangakis

  • Article |

    Respirasomes are supercomplexes of mitochondrial electron transport chain complexes that are responsible for cellular respiration and energy production; a cryo-electron microscopy structural study of the respirasome is presented.

    • Jinke Gu
    • , Meng Wu
    •  & Maojun Yang

  • Letter |

    The high-resolution cryo-electron microscopy structure of the kainate receptor GluK2 subtype in its desensitized state is reported, which reveals that desensitization is attained by establishing a ring-like structure in the ligand-binding domains.

    • Joel R. Meyerson
    • , Sagar Chittori
    •  & Sriram Subramaniam

  • Article |

    A high-resolution structure of a complex between the anaphase-promoting complex (APC/C) and the mitotic checkpoint complex (MCC) reveals how MCC interacts with and represses APC/C by obstructing substrate recognition and suppressing E3 ligase activity.

    • Claudio Alfieri
    • , Leifu Chang
    •  & David Barford

  • Letter |

    Electron cryomicroscopy structures are provided for all core and supernumerary protein subunits of mammalian complex I, a 45-subunit enzyme that powers eukaryotic respiration.

    • Jiapeng Zhu
    • , Kutti R. Vinothkumar
    •  & Judy Hirst

  • Letter |

    A cryo-electron microscopy structure of the DNA damage repair protein 53BP1 bound to a nucleosome illuminates the way 53BP1 recognizes two types of histone modifications (a methyl group and a ubiquitin moiety), and provides insight into the highly specified recognition and recruitment of 53BP1 to modified chromatin.

    • Marcus D. Wilson
    • , Samir Benlekbir
    •  & Daniel Durocher

  • Article |

    Cryo-electron microscopy has undergone a resolution revolution—here, this method has been combined with lipid nanodisc technology to solve structures of TRPV1, the receptor for capsaicin, in a membrane bilayer, revealing mechanisms of lipid and ligand regulation.

    • Yuan Gao
    • , Erhu Cao
    •  & Yifan Cheng

  • Article |

    Cryo-electron microscopy structural models of the human pre-initiation complex at all major steps of transcription initiation at near atomic-level resolution are presented, providing new mechanistic insights into the processes of promoter melting and transcription-bubble formation, as well as an almost complete proposed structural model of all of the pre-initiation complex components and their interactions with DNA.

    • Yuan He
    • , Chunli Yan
    •  & Eva Nogales

  • Article |

    The cryo-electron microscopy structures of yeast initiation complexes containing the transcription factors TBP, TFIIA, TFIIB, TFIIE, and TFIIF and containing either closed or open promoter DNA are reported, providing mechanistic insights into DNA opening and template-strand loading.

    • C. Plaschka
    • , M. Hantsche
    •  & P. Cramer

  • Letter |

    The structure of a bacterial ribosome–RelA complex reveals that RelA, a protein recruited to the ribosome in the case of scarce amino acids, binds in a different location to translation factors, and that this binding event suppresses auto-inhibition to activate synthesis of the (p)ppGpp secondary messenger, thus initiating stringent control.

    • Alan Brown
    • , Israel S. Fernández
    •  & V. Ramakrishnan

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