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How good can cryo-EM become?

Nature Methods volume 13, pages 28–32 (2016)Cite this article

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Abstract

The suddenness with which single-particle cryo-electron microscopy (cryo-EM) has emerged as a method for determining high-resolution structures of biological macromolecules invites the questions, how much better can this technology get, and how fast is that likely to happen? Though we can rightly celebrate the maturation of cryo-EM as a high-resolution structure-determination tool, I believe there still are many developments to look forward to.

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Figure 1: Comparison of cryo-EM images of recombinant Thermoplasma acidophilum 20S proteasomes.

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Acknowledgements

The writing of this commentary has been supported in part by US National Institutes of Health grant GM083039. I want to especially thank R. Danev for providing the pair of images used to prepare Figure 1.

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  1. Robert M. Glaeser is at the Lawrence Berkeley National Laboratory, University of California, Berkeley, California, USA.,

    Robert M Glaeser

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  1. Robert M Glaeser
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Correspondence to Robert M Glaeser.

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Glaeser, R. How good can cryo-EM become?. Nat Methods 13, 28–32 (2016). https://doi.org/10.1038/nmeth.3695

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