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Cited by 13RNA and protein synthesis mechanismsAdvanced Electron Microscopy Techniques and ApplicationsEnzyme Structure and Function

Capturing ribosomal structures in cellular extracts with cryoPRISM: A purification-free cryoEM approach reveals novel structural states

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May, Mira B., Lopez-Perez, Gabriella S., Davis, Joseph H.·2026·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.2521210123PMC PMC12956868
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Abstract

Structural analyses of ribosomes by single particle cryogenic electron microscopy (cryoEM) have traditionally relied on purified or reconstituted samples, with particles often trapped in desired states using genetic, pharmacological, or biochemical perturbations. While informative, such in vitro methods often fail to capture the full diversity of structural states and associated protein factors present in cells. In contrast, in situ cryoelectron tomography preserves cellular context but is limited by low throughput and modest resolution. Here, we present cryoPRISM (purification-free ribosome imaging from subcellular mixtures), a rapid ex vivo workflow encompassing cell lysis, vitrification, and image analysis methods for high-resolution analyses of ribosomal structures directly from cell lysates. Applying cryoPRISM in Escherichia coli , we resolved more than 20 distinct ribosomal states spanning assembly, translation initiation, elongation, trans-translation, and quiescence, including a novel configuration of EF-G bound to idle ribosomes with the ribosome hibernation factor ribosome-associated inhibitor A. Given its speed, accessibility, and ability to preserve native interactions and structural heterogeneity, we anticipate that cryoPRISM will be broadly applicable for uncovering ribosomal biology across diverse organisms and conditions.

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Sorted by citations

Authors
May, M. B., Lopez-Perez, G. S., & Davis, J. H.
Affiliations
Massachusetts Institute of Technology (US)
Corresponding author
  • May, Mira B.
  • Lopez-Perez, Gabriella S.
  • Davis, Joseph H.
ORCID
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2026-02-25
Volume
123
Issue
9
Pages
e2521210123-e2521210123
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.2521210123
PMC
PMC12956868
OpenAlex
W7131402317
Cited by
13
References
2
Citations by year
2026: 13
FWCI
22.32
Type
journal article
Language
en
Open access
Licence
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion, cc-by-nc-nd)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • PubMed Central (publishedVersion, cc-by-nc-nd)
  • PubMed Central (submittedVersion, cc-by-nc-nd)
Funders
  • HHS | NIH | National Institute of General Medical Sciences (R01GM144542)
  • NSF (CAREER grant 2046778, GRFP)
  • Richard and Susan Smith Family Foundation (Odyssey Award)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords
ribosome structure, cell lysate, elongation factor G, ribosome hibernation, translation initiation, translation elongation, trans-translation, ribosome assembly, Escherichia coli, structural heterogeneity

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