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2017 Nobel Prize in Chemistry

Nature Research congratulates the awardees of the 2017 Nobel Prize in Chemistry - Jacques Dubochet, Joachim Frank and Richard Henderson. Their pioneering work on the use of cryo-electron microscopy to solve high-resolution structures of biomolecules has provided unprecedented insights into the complexity of life. Here, we present a Collection of Research, Methods, Reviews and Comment pieces from Nature Research to celebrate the award.

From the Laureates

Reviews, News and Comment

Methods and Protocols


  • Nature | 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
    • , David Julius
    •  &  Yifan Cheng
  • Nature | 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
    • , Yifan Cheng
    •  &  David Julius
  • Nature | Article

    A 3.7 Å resolution structure for the yeast U4/U6.U5 tri-snRNP, a complex involved in splicing, allows a better appreciation of the architecture of the tri-snRNP, and offers new functional insights into the activation of the spliceosome and the assembly of the catalytic core.

    • Thi Hoang Duong Nguyen
    • , Wojciech P. Galej
    • , Xiao-chen Bai
    • , Chris Oubridge
    • , Andrew J. Newman
    • , Sjors H. W. Scheres
    •  &  Kiyoshi Nagai
  • Nature | 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
    • , Amélie Fradet-Turcotte
    • , Alana Sherker
    • , Jean-Philippe Julien
    • , Andrea McEwan
    • , Sylvie M. Noordermeer
    • , Frank Sicheri
    • , John L. Rubinstein
    •  &  Daniel Durocher