4.6 Article

Cryo-EM is a powerful tool, but helical applications can have pitfalls

Journal

SOFT MATTER
Volume 17, Issue 12, Pages 3291-3293

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/d1sm00282a

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Funding

  1. NIH [GM122510]

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The paper examines the use of cryo-electron microscopy to analyze polymorphic helical tubes formed by a tetrameric protein, highlighting the potential and pitfalls of this technique when determining complex structures at subatomic resolutions. The study emphasizes the importance of reaching near-atomic resolution to accurately model complex assemblies.
In structural biology, cryo-electron microscopy (cryo-EM) has emerged as the main technique for determining the atomic structures of macromolecular complexes. This has largely been due to the introduction of direct electron detectors, which have allowed for routinely reaching a near-atomic resolution when imaging such complexes. In chemistry and materials science, the applications of cryo-EM have been much more limited. A recent paper (Z. Li et al., Chemically Controlled Helical Polymorphism In Protein Tubes By Selective Modulation Of Supramolecular Interactions, J. Am. Chem. Soc. 2019, 141, 19448-19457) has used low resolution cryo-EM to analyze polymorphic helical tubes formed by a tetrameric protein, and has made detailed models for the interfaces between the tetramers in these assemblies. Due to intrinsic ambiguities in determining the correct helical symmetry, we show that many of the models are likely to be wrong. This note highlights both the enormous potential for using cryo-EM, and also the pitfalls possible for helical assemblies when a near-atomic level of resolution is not reached.

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