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Unravelling biological macromolecules with cryo-electron microscopy

Author

Listed:
  • Rafael Fernandez-Leiro

    (MRC Laboratory of Molecular Biology, Cambridge Biomedical Campus)

  • Sjors H. W. Scheres

    (MRC Laboratory of Molecular Biology, Cambridge Biomedical Campus)

Abstract

Knowledge of the three-dimensional structures of proteins and other biological macromolecules often aids understanding of how they perform complicated tasks in the cell. Because many such tasks involve the cleavage or formation of chemical bonds, structural characterization at the atomic level is most useful. Developments in the electron microscopy of frozen hydrated samples (cryo-electron microscopy) are providing unprecedented opportunities for the structural characterization of biological macromolecules. This is resulting in a wave of information about processes in the cell that were impossible to characterize with existing techniques in structural biology.

Suggested Citation

  • Rafael Fernandez-Leiro & Sjors H. W. Scheres, 2016. "Unravelling biological macromolecules with cryo-electron microscopy," Nature, Nature, vol. 537(7620), pages 339-346, September.
    • Handle: RePEc:nat:nature:v:537:y:2016:i:7620:d:10.1038_nature19948
    DOI: 10.1038/nature19948
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    Cited by:

    1. Xu Han & Dongliang Zhang & Lu Hong & Daqi Yu & Zhaolong Wu & Tian Yang & Michael Rust & Yuhai Tu & Qi Ouyang, 2023. "Determining subunit-subunit interaction from statistics of cryo-EM images: observation of nearest-neighbor coupling in a circadian clock protein complex," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    2. Shivali Patel & Alec N. Sexton & Madison S. Strine & Craig B. Wilen & Matthew D. Simon & Anna Marie Pyle, 2023. "Systematic detection of tertiary structural modules in large RNAs and RNP interfaces by Tb-seq," Nature Communications, Nature, vol. 14(1), pages 1-11, December.

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