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Advances in the field of single-particle cryo-electron microscopy over the last decade

Nature Protocols volume 12, pages 209–212 (2017)Cite this article

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Abstract

In single-particle cryo-electron microscopy (cryo-EM), molecules suspended in a thin aqueous layer are rapidly frozen and imaged at cryogenic temperature in the transmission electron microscope. From the random projection views, a three-dimensional image is reconstructed, enabling the structure of the molecule to be obtained. In this article I discuss technological progress over the past decade, which has, in my own field of study, culminated in the determination of ribosome structure at 2.5-Å resolution. I also discuss likely future improvements in methodology.

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Figure 1
Figure 2: Improvements in resolution of the ribosome structure over the past decade.

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Acknowledgements

This work has been supported by the Howard Hughes Medical Institute and by US National Institutes of Health grant R01 GM29169.

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  1. Departments of Biochemistry and Molecular Biophysics and of Biological Sciences, Columbia University, New York, New York, USA

    Joachim Frank

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Correspondence to Joachim Frank.

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Frank, J. Advances in the field of single-particle cryo-electron microscopy over the last decade. Nat Protoc 12, 209–212 (2017). https://doi.org/10.1038/nprot.2017.004

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