Cryoelectron microscopy articles within Nature

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  • Letter |

    The first high-resolution, cryo-electron microscopy structure of mammalian RNA polymerase II, in the form of a transcribing complex comprising DNA template and RNA transcript.

    • Carrie Bernecky
    • , Franz Herzog
    •  & Patrick Cramer

  • Article |

    RNA polymerase III (Pol III), the largest eukaryote polymerase yet characterized, transcribes structured small non-coding RNAs; here cryo-electron microscopy structures of budding yeast Pol III allow building of an atomic-level model of the complete 17-subunit complex, both unbound and while elongating RNA.

    • Niklas A. Hoffmann
    • , Arjen J. Jakobi
    •  & Christoph W. Müller

  • Article |

    This study has determined the electron cryomicroscopy structure of the mammalian type 1 InsP3 receptor in a ligand-free state at 4.7 Å resolution; although the central Ca2+-conduction pathway is similar to other ion channels, the unique architecture of the C-terminal domains of the tetrameric channel suggests that a distinctive allosteric mechanism underlies the activation of InsP3 gating.

    • Guizhen Fan
    • , Matthew L. Baker
    •  & Irina I. Serysheva

  • Article |

    Piezo1, a mechanosensitive cation channel, senses shear stress of blood flow for proper blood vessel development, regulates red blood cell function and controls cell migration and differentiation; here a trimeric architecture of this novel class of ion channel is reported, suggesting that Piezo1 may use its peripheral propeller-like ‘blades’ as force sensors to gate the central ion-conducting pore.

    • Jingpeng Ge
    • , Wanqiu Li
    •  & Maojun Yang

  • Article |

    The cryo-electron microscopy structure of the eukaryotic initiation factor 3 (eIF3) within the larger 43S complex is determined; the improved resolution enables visualization of the secondary structures of the subunits, as well as the contacts between eIF3 and both eIF2 and DHX29.

    • Amedee des Georges
    • , Vidya Dhote
    •  & Yaser Hashem

  • Article |

    The atomic structure of human γ-secretase at 3.4 Å resolution, determined by single-particle cryo-electron microscopy.

    • Xiao-chen Bai
    • , Chuangye Yan
    •  & Yigong Shi

  • Letter |

    All eukaryotes utilize a single termination factor, eRF1, to halt translation when the ribosome encounters one of three possible stop codons; here electron cryo-microscopy structures of ribosome–eRF1 complexes in the process of recognizing each stop codon reveal how stop codons are discriminated from sense codons.

    • Alan Brown
    • , Sichen Shao
    •  & V. Ramakrishnan

  • Article |

    Cryo-electron microscopy is used to visualize the double hexamer of the eukaryotic minichromosome maintenance complex (MCM), which is assembled during the G1 phase of DNA replication; two interdigitated hexamers have a central channel that tightly fits a DNA duplex, and the orientation of the tilted single hexamers sheds light on many functional aspects, particularly in the initial origin DNA melting.

    • Ningning Li
    • , Yuanliang Zhai
    •  & Ning Gao

  • Article |

    This study determines the structure of the spliceosomal tri-snRNP complex (containing three small nuclear RNAs and more than 30 proteins) by single-particle cryo-electron microscopy; the resolution is sufficient to discern the organization of RNA and protein components involved in spliceosome activation, exon alignment and catalysis.

    • Thi Hoang Duong Nguyen
    • , Wojciech P. Galej
    •  & Kiyoshi Nagai

  • Letter |

    Retroviruses such as HIV rely on the intasome, a tetramer of integrase protein bound to the viral DNA ends interacting with host chromatin, for integration into the host genome; the structure of the intasome as it interacts with a nucleosome is now solved, giving insight into the integration process.

    • Daniel P. Maskell
    • , Ludovic Renault
    •  & Peter Cherepanov

  • Article |

    The structure of the human ribosome at high resolution has been solved; by combining single-particle cryo-EM and atomic model building, local resolution of 2.9 Å was achieved within the most stable areas of the structure.

    • Heena Khatter
    • , Alexander G. Myasnikov
    •  & Bruno P. Klaholz

  • Letter |

    A single particle cryo-EM structure of the 70S ribosome in complex with the elongation factor Tu breaks the 3 Å resolution barrier of the technique and locally exceeds the resolution of previous crystallographic studies, revealing all modifications in rRNA and explaining their roles in ribosome function and antibiotic binding.

    • Niels Fischer
    • , Piotr Neumann
    •  & Holger Stark

  • Article |

    Using single-particle electron cryomicroscopy, several structures are reported which illuminate the mechanisms of action of the ATPase NSF that disassembles the SNARE complex into individual protein components.

    • Minglei Zhao
    • , Shenping Wu
    •  & Axel T. Brunger

  • Article |

    Using electron cryomicroscopy, the structure of the closed-state rabbit ryanodine receptor RyR1 in complex with its modulator FKBP12 is solved at 3.8 Å; in addition to determining structural details of the ion-conducting channel domain, three previously uncharacterized domains help to reveal a molecular scaffold that allows long-range allosteric regulation of channel activities.

    • Zhen Yan
    • , Xiao-chen Bai
    •  & Nieng Yan

  • Article |

    Using electron cryomicroscopy, the closed-state structure of rabbit RyR1 is determined at 4.8 Å resolution; analysis confirms that the RyR1 architecture consists of a six-transmembrane ion channel with a cytosolic α-solenoid scaffold, and suggests a mechanism for Ca2+-induced channel opening.

    • Ran Zalk
    • , Oliver B. Clarke
    •  & Andrew R. Marks

  • Letter |

    Electron cryomicroscopy reveals the three-dimensional structure of F-actin at a resolution of 3.7 Å in complex with tropomyosin at a resolution of 6.5 Å; the stabilizing interactions and the effects of disease-causing mutants are also investigated.

    • Julian von der Ecken
    • , Mirco Müller
    •  & Stefan Raunser

  • Article |

    Using electron cryomicroscopy, the structure of the rabbit RyR1 calcium channel is determined at 6.1 Å resolution in the closed state and 8.5 Å in the open state, revealing how calcium binding to the EF-hand of RyR1 regulates channel opening and facilitates calcium-induced calcium release.

    • Rouslan G. Efremov
    • , Alexander Leitner
    •  & Stefan Raunser

  • Letter |

    The structure of the 39S large mitoribosome subunit is solved by cryo-electron microscopy at an impressive 3.4 Å resolution, revealing the location of 50 ribosomal proteins, the peptidyl transferase centre, the tRNAs within this active site, and the nascent peptide chain within the exit tunnel.

    • Basil J. Greber
    • , Daniel Boehringer
    •  & Nenad Ban

  • Article |

    Complex I is the first enzyme of the mitochondrial electron transport chain and it is essential for oxidative phosphorylation in mammalian mitochondria; here the electron cryo-microscopy structure of complex I from bovine heart mitochondria is reported, advancing knowledge of its structure in mammals.

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

  • Article |

    The anaphase-promoting complex/cyclosome (APC/C) is a large E3 ligase that mediates ubiquitin-dependent proteolysis of cell cycle regulatory proteins; here the complete secondary structure architecture of human APC/C complexed with its coactivator CDH1 and substrate HSL1 is determined at 7.4 Å resolution, revealing allosteric changes induced by the coactivator that enhance affinity for UBCH10–ubiqutin.

    • Leifu Chang
    • , Ziguo Zhang
    •  & David Barford

  • Article |

    The three-dimensional structure of intact human γ-secretase complex at 4.5 Å resolution is revealed by cryo-electron-microscopy single-particle analysis; the complex comprises a horseshoe-shaped transmembrane domain containing 19 transmembrane segments, and a large extracellular domain from nicastrin, which sits immediately above the hollow space formed by the horseshoe.

    • Peilong Lu
    • , Xiao-chen Bai
    •  & Yigong Shi

  • Letter |

    Polyketide synthases (PKSs) are multidomain enzymes that produce polyketides, which form the basis of many therapeutic agents; here, electron cryo-microscopy is used to probe the structure of an intact module of a multi-enzyme PKS in different functional states.

    • Jonathan R. Whicher
    • , Somnath Dutta
    •  & Georgios Skiniotis

  • Article |

    Polyketide synthases are multidomain enzymes that produce polyketides, which form the basis of many therapeutic agents; here, electron cryo-microscopy is used to establish the structure of a bacterial full-length module, and to elucidate the structural basis of both intramodule and intermodule substrate transfer.

    • Somnath Dutta
    • , Jonathan R. Whicher
    •  & Georgios Skiniotis

  • Letter |

    Many bacteria are able to survive in the presence of antibiotics in part because they possess pumps that can remove a broad range of small molecules; here, the structure of one such pump, AcrAB–TolC, is determined using X-ray crystallography and cryo-electron microscopy.

    • Dijun Du
    • , Zhao Wang
    •  & Ben F. Luisi

  • Article |

    High-resolution structures of the Photorhabdus luminescens TcA toxin subunit and the entire Tc toxin complex reveal important new insights into Tc complex structure and function.

    • Dominic Meusch
    • , Christos Gatsogiannis
    •  & Stefan Raunser

  • Letter |

    Nascent secretory and membrane proteins are targeted to the Sec61 protein-conducting channel for translocation across or insertion into the endoplasmic reticulum membrane; here cryo-electron microscopy structures of eukaryotic ribosome–channel complexes show how this channel opens vertically during translocation of a secretory protein into the lumen of the endoplasmic reticulum and how it opens laterally during insertion of a transmembrane domain into the lipid bilayer.

    • Marko Gogala
    • , Thomas Becker
    •  & Roland Beckmann

  • Article |

    Cryo-electron microscopy combined with chemical crosslinking and mass spectrometry is used to determine the structure of the large subunit of the mammalian mitoribosome; this structure provides detailed structural insight, particularly of the molecular architecture of the polypeptide exit site, which has been structurally remodelled during evolution, presumably to help facilitate the membrane insertion of the highly hydrophobic proteins encoded by the mitochondrial genome.

    • Basil J. Greber
    • , Daniel Boehringer
    •  & Nenad Ban

  • Article |

    Using a peptide toxin and small vanilloid agonists as pharmacological probes, high-resolution electron cryo-microscopy structures of rat TRPV1–ligand complexes are solved; these structures highlight conformational differences between TRP and voltage-gated ion channels in their active states, and suggest a dual gating mechanism that may account for the ability of members of the TRP channel superfamily to integrate diverse physiological signals.

    • Erhu Cao
    • , Maofu Liao
    •  & David Julius

  • Article |

    A high-resolution electron cryo-microscopy structure of the rat transient receptor potential (TRP) channel TRPV1 in its ‘closed’ state is presented; the overall structure of this ion channel is found to share some common features with voltage-gated ion channels, although several unique, TRP-specific features are also characterized.

    • Maofu Liao
    • , Erhu Cao
    •  & Yifan Cheng

  • Letter |

    Newly synthesized proteins are targeted to the SecY protein-conducting channel for translocation across the membrane; here, cryo-electron microscopy structures of inactive and active ribosome–channel complexes are presented, revealing that ribosome binding does not result in major structural changes to transmembrane regions of the channel, and that stable channel opening requires loop insertion of the translocating nascent chain.

    • Eunyong Park
    • , Jean-François Ménétret
    •  & Christopher W. Akey

  • 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

  • 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

  • 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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