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Stroboscopic imaging of macromolecular complexes

Nature Methods volume 10, pages 475–476 (2013)Cite this article

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Two reports describing the use of direct-conversion electron detectors and algorithms that correct for beam-induced sample motion in single-particle electron cryomicroscopy demonstrate that this technique can solve structures of macromolecules at near-atomic resolution.

Two remarkable advances have just been made in the use of single-particle electron cryomicroscopy (cryo-EM) to image macromolecular complexes at high resolution. Reporting in eLife, Bai et al.1 imaged the 80S ribosome from yeast (Saccharomyces cerevisiae) at an overall resolution of 4.5 Å. This is an unprecedented achievement for the structure determination of asymmetric macromolecular complexes that lack multiple copies of identical subunits. This was accomplished by merging data from images of only 30,000 ribosome particles, about 50–100 times fewer particles than were used in previous work. In this issue of Nature Methods, Li et al.2 report that a much smaller particle, the 20S proteasome from Thermoplasma acidophilum, was imaged at a resolution of 3.3 Å. For comparison, the highest resolution achieved in previous cryo-EM studies of the Thermoplasma proteasome was about 5.6 Å. The 14-fold symmetry of the 20S proteasome could be exploited in this case; as a result, nearly the full resolution was reached after the authors merged data from only 16,000 proteasome particles (224,000 asymmetric units).

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Figure 1: Obtaining high-resolution density maps by single-particle cryo-EM does not require crystals of large, macromolecular structures.

Katie Vicari

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  1. Robert M. Glaeser is in the Life Sciences Division, 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. Stroboscopic imaging of macromolecular complexes. Nat Methods 10, 475–476 (2013). https://doi.org/10.1038/nmeth.2486

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