Cryoelectron microscopy articles within Nature

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  • Article
    | Open Access

    Through structural analysis of the activation of bacterial STING, the molecular basis of STING filament formation and TIR effector domain activation in antiphage signalling is defined.

    • Benjamin R. Morehouse
    • , Matthew C. J. Yip
    •  & Philip J. Kranzusch

  • Article |

    The cryo-electron microscopy structure of the filamentous hydrogen-dependent CO2 reductase (HDCR) enzyme from Thermoanaerobacter kivui, together with enzymatic analysis and in situ cryo-electron tomography, provides insight into the high catalytic activity of HDCR.

    • Helge M. Dietrich
    • , Ricardo D. Righetto
    •  & Jan M. Schuller

  • Article
    | Open Access

    The Csu pili of the multidrug-resistant nosocomial pathogen Acinetobacter baumannii assemble into an ultrathin zigzag architecture secured by a clinch mechanism that provides the pilus with high mechanical stability and superelasticity.

    • Natalia Pakharukova
    • , Henri Malmi
    •  & Anton V. Zavialov

  • Article |

    The 3D structure of the human nutrient-sensing complex GATOR2 is resolved using cryo-electron microscopy.

    • Max L. Valenstein
    • , Kacper B. Rogala
    •  & David M. Sabatini

  • Article
    | Open Access

    Cryo-electron microscopy structure, molecular dynamics and biochemical analyses of the SHOC2–PP1C–MRAS complex demonstrate the dependence of the complex formation on RAS–GTP and identify the determinants of RAS isoform preference for SHOC2–PP1C and specificity of the complex for RAF dephosphorylation.

    • Nicholas P. D. Liau
    • , Matthew C. Johnson
    •  & Jawahar Sudhamsu

  • Article
    | Open Access

    Structures of the Dcr-2–Loqs-PD complex while it is processing a double-stranded RNA (dsRNA) substrate elucidate the interactions between Dcr-2 and Loqs-PD, and show that Dcr-2 undergoes substantial conformational changes during a dsRNA-processing cycle.

    • Shichen Su
    • , Jia Wang
    •  & Jinbiao Ma

  • Article
    | Open Access

    Cryo-electron microscopy structures of Drosophila Dicer-2–R2D2 complexes with and without small interfering RNA reveal how the RNA is presented to Argonaute in the correct orientation for viral gene silencing.

    • Sonomi Yamaguchi
    • , Masahiro Naganuma
    •  & Osamu Nureki

  • Article |

    Single-molecule spectroscopy and structural studies were used to examine the dynamics of association of eIF1A and eIF5B with the human translation initiation complex and their role in presenting tRNA to the complex to initiate translation.

    • Christopher P. Lapointe
    • , Rosslyn Grosely
    •  & Joseph D. Puglisi

  • Article
    | Open Access

    Cryo-electron microscopy structures of a 2.8 megadalton bacterial type IV secretion system encoded by the plasmid R388 and comprising 92 polypeptides provide insights into the stepwise mechanism of pilus assembly.

    • Kévin Macé
    • , Abhinav K. Vadakkepat
    •  & Gabriel Waksman

  • Article
    | Open Access

    Cryo-electron microscopy structures of the sequential assembly of the CMG replicative helicase on a chromatinized origin of replication provide insights into the mechanism through which DNA melting is initiated by ATP binding.

    • Jacob S. Lewis
    • , Marta H. Gross
    •  & Alessandro Costa

  • Article |

    Structural determination of GAT1 using cryo-electron microscopy provides insights into the biology and pharmacology of this GABA transporter.

    • Zenia Motiwala
    • , Nanda Gowtham Aduri
    •  & Cornelius Gati

  • Article |

    Cryo-electron microscopy structures of the bile acid transporter NTCP in the apo state and in complex with the preS1 domain of hepatitis B virus (HBV) provide insight into NTCP substrate transport and HBV recognition mechanisms.

    • Jinta Asami
    • , Kanako Terakado Kimura
    •  & Umeharu Ohto

  • Article |

    Cryo-electron microscopy and crystal structures of Arabidopsis NPR1—a bird-shaped homodimer—and its complex with the transcription factor TGA3 provide an explanation for a direct role of salicylic acid and enhanceosome assembly in regulating NPR1-dependent gene expression.

    • Shivesh Kumar
    • , Raul Zavaliev
    •  & Pei Zhou

  • Article
    | Open Access

    Structural studies of human Na+–taurocholate co-transporting polypeptide in complex with nanobodies reveal mechanisms for bile salts transport and HBV recognition involving an open-pore intermediate state.

    • Kapil Goutam
    • , Francesco S. Ielasi
    •  & Nicolas Reyes

  • Article
    | Open Access

    Cryo-EM structures of AMPA receptor with the subunit γ2 in non-desensitizing conditions at low glutamate concentrations disprove the one-to-one link between the number of glutamate-bound subunits and ionotropic glutamate receptor conductance.

    • Maria V. Yelshanskaya
    • , Dhilon S. Patel
    •  & Alexander I. Sobolevsky

  • Article |

    Cryo-electron microscopy structures of GPR56 and latrophilin 3 show how the released tethered agonist peptide interacts with the transmembrane domain, suggesting a model for the activation mechanism of adhesion G-protein-coupled receptors.

    • Ximena Barros-Álvarez
    • , Robert M. Nwokonko
    •  & Georgios Skiniotis

  • Article |

    Cryo-electron microscopy structures of the bacterial O-antigen ligase WaaL, combined with genetics, biochemistry and molecular dynamics simulations, provide insight into the mechanism by which WaaL catalyses the biosynthesis of lipopolysaccharide.

    • Khuram U. Ashraf
    • , Rie Nygaard
    •  & Filippo Mancia

  • Article |

    The cryo-electron microscopy structure of human STING bound to both cyclic GMP-AMP and the small-molecule agonist C53 reveals an agonist-binding site in the STING transmembrane domain, and provides insight into the oligomerization and activation of STING.

    • Defen Lu
    • , Guijun Shang
    •  & Xuewu Zhang

  • Article |

    A cryo-electron microscopy analysis reveals how HAS selects its substrates, hydrolyses the first substrate to prime the synthesis reaction, opens a hyaluronan-conducting transmembrane channel, ensures alternating substrate polymerization and coordinates hyaluronan inside its transmembrane pore.

    • Finn P. Maloney
    • , Jeremi Kuklewicz
    •  & Jochen Zimmer

  • Article
    | Open Access

    A study using structure determination by cryogenic electron microscopy identifies and characterizes TMEM106B amyloid filaments in human brain, and suggests that their formation is age dependent, with no obvious association with disease.

    • Manuel Schweighauser
    • , Diana Arseni
    •  & Sjors H. W. Scheres

  • Article
    | Open Access

    Cryo-electron microscopy structures of ligand-free, agonist-bound and antagonist-bound Ste2 show that this class D1 G protein-coupled receptor has a distinct mechanism of activation compared with other receptor classes.

    • Vaithish Velazhahan
    • , Ning Ma
    •  & Christopher G. Tate

  • Article
    | Open Access

    Cryo-electron microscopy structures of Cas9 during mismatch cleavage provide insight into the mechanisms that control off-target effects of Cas9, which will aid in the future design of high-fidelity Cas9 variants with reduced off-target cleavage.

    • Jack P. K. Bravo
    • , Mu-Sen Liu
    •  & David W. Taylor

  • Article |

    The structures of the open and closed states of the Omicron spike protein and its complex with the ACE2 receptor or a broadly neutralizing antibody are resolved and shed light on the receptor engagement and antibody neutralization of Omicron.

    • Qin Hong
    • , Wenyu Han
    •  & Yao Cong

  • Article |

    The cryo-electron microscopy structure of the glucocorticoid receptor (GR)-loading complex—a complex in which Hsp70 loads GR onto Hsp90 and Hop—is described, providing insights into how the chaperones Hsp90 and Hsp70 coordinate to facilitate GR remodelling for activation.

    • Ray Yu-Ruei Wang
    • , Chari M. Noddings
    •  & David A. Agard

  • Article |

    Unphosphorylated PINK1 of Pediculus humanus corporis forms a dimerized state before undergoing trans-autophosphorylation, and phosphorylated PINK1 undergoes a conformational change in the N-lobe to produce its phosphorylated, ubiquitin-binding state.

    • Zhong Yan Gan
    • , Sylvie Callegari
    •  & David Komander

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