ArticleProceedings of the National Academy of Sciences of the United States of America2025
Reducing the effects of radiation damage in cryo-EM using liquid helium temperatures.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- High-resolution nuclear cell biology by cryo-electron tomography.Nucleus (Austin, Tex.) · 2026Review
- Optimized cryo-FIB milling strategy to generate thin, minimally damaged biological lamellae.bioRxiv : the preprint server for biology · 2026Article
- Review
- Cryo-EM: the revolution continues.IUCrJ · 2026Review
- Pulsed-electron illumination does not reduce beam damage for imaging biological macromolecules.Nature communications · 2026Article
- Damage-limited resolution for X-ray and electron microscopy of organic specimens.Acta crystallographica. Section D, Structural biology · 2026Article
- A Surfactant Cocktail Overcomes Air-Water Interface Artifacts in Single-Particle CryoEM.bioRxiv : the preprint server for biology · 2026Article
- Ultracold cryogenic TEM with liquid helium and high stability.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Extending the reach of single-particle cryoEM.Current opinion in structural biology · 2025Review
- Reducing the effects of radiation damage in cryo-EM using liquid helium temperatures.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
The physical limit in determining the atomic structure of biological molecules is radiation damage. In electron cryomicroscopy, there have been numerous attempts to reduce the effects of radiation damage by cooling the specimen beyond liquid-nitrogen temperatures, yet all failed to realize the potential improvement for single-particle structure determination. We have identified the physical causes of information loss at liquid-helium temperatures, and overcome them using a combination of nanoscale electron beam illumination and a gold specimen support with 100 nm diameter holes. This combination allowed structure determination where every frame in the exposure contained more information than was available with cryomicroscopy at liquid-nitrogen temperatures, matching expectations from crystal diffraction. Since a 100 nm hole is smaller than the field of view of a typical micrograph, the edges of the foil are directly visible in each micrograph. Protein molecules that are degraded tend to aggregate at the edges of foil holes and can constitute a significant fraction of the micrograph. This and the need for minimal water-foil irradiation will both be important to consider as new cryomicroscopes and specimen supports are developed for imaging molecules at extremely low temperatures where the effects of radiation damage are reduced.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.