Cryoelectron microscopy

Definition

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.

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Latest Research and Reviews

  • Research |

    A high-resolution structure of the human ribosome determined by cryo-electron microscopy visualizes numerous RNA modifications that are concentrated at functional sites with an extended shell, and suggests the possibility of designing more specific ribosome-targeting drugs.

    • S. Kundhavai Natchiar
    • , Alexander G. Myasnikov
    • , Hanna Kratzat
    • , Isabelle Hazemann
    •  & Bruno P. Klaholz
  • Research | | open

    Leishmaniasis is a parasitic disease transmitted by the bite of infected sand flies. Here the authors describe an atomic resolution cryo-EM structure of the Leishmania ribosome in complex with the recently approved drug paromomycin (PAR) and highlight conserved elements in the drug binding pocket that mediate PAR deleterious effects on the parasite.

    • Moran Shalev-Benami
    • , Yan Zhang
    • , Haim Rozenberg
    • , Yuko Nobe
    • , Masato Taoka
    • , Donna Matzov
    • , Ella Zimmerman
    • , Anat Bashan
    • , Toshiaki Isobe
    • , Charles L. Jaffe
    • , Ada Yonath
    •  & Georgios Skiniotis
  • Research | | open

    The transcription co-activator complex SAGA is recruited to promoters by transcriptional activators and promotes the formation of the pre-initiation complex. Here, the authors present the cryo-EM structure of the SAGA complex and resolve the major target of activator binding, the 430 kDa Tra1 protein.

    • Grigory Sharov
    • , Karine Voltz
    • , Alexandre Durand
    • , Olga Kolesnikova
    • , Gabor Papai
    • , Alexander G. Myasnikov
    • , Annick Dejaegere
    • , Adam Ben Shem
    •  & Patrick Schultz
  • Research |

    Electron cryo-microscopy structures of the human peptide-loading complex shed light on its operation and on the onset of adaptive immune responses.

    • Andreas Blees
    • , Dovile Januliene
    • , Tommy Hofmann
    • , Nicole Koller
    • , Carla Schmidt
    • , Simon Trowitzsch
    • , Arne Moeller
    •  & Robert Tampé
  • Research | | open

    CRISPR-Cas9 is widely used for genome engineering but structural data for the DNA cleavage step are still incomplete. Here, the authors present the cryo-EM structure of a ternary Cas9-sgRNA-target DNA complex, perform MD simulations and discuss implications for the Cas9 DNA cleavage mechanism.

    • Cong Huai
    • , Gan Li
    • , Ruijie Yao
    • , Yingyi Zhang
    • , Mi Cao
    • , Liangliang Kong
    • , Chenqiang Jia
    • , Hui Yuan
    • , Hongyan Chen
    • , Daru Lu
    •  & Qiang Huang

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