ArticleActa crystallographica. Section D, Structural biology2022
Microsecond melting and revitrification of cryo samples: protein structure and beam-induced motion.
Article in Acta crystallographica. Section D, Structural biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Integrating multitemperature sample preparation with particle rebalancing addresses preferred orientation.PNAS nexus · 2026Article
- Advancing time-resolved structural biology: latest strategies in cryo-EM and X-ray crystallography.Nature methods · 2025Review
- Embracing Heterogeneity: Challenging the Paradigm of Replisomes as Deterministic Machines.Chemical reviews · 2023Review
- Fast viral dynamics revealed by microsecond time-resolved cryo-EM.Nature communications · 2023Article
- Near-atomic resolution reconstructions from in situ revitrified cryo samples.Acta crystallographica. Section D, Structural biology · 2023Article
- Electron diffraction of deeply supercooled water in no man's land.Nature communications · 2023Article
- Frozen in time: analyzing molecular dynamics with time-resolved cryo-EM.Structure (London, England : 1993) · 2023Review
- Microsecond melting and revitrification of cryo samples with a correlative light-electron microscopy approach.Frontiers in molecular biosciences · 2022Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
A novel approach to time-resolved cryo-electron microscopy (cryo-EM) has recently been introduced that involves melting a cryo sample with a laser beam to allow protein dynamics to briefly occur in the liquid, before trapping the particles in their transient configurations by rapidly revitrifying the sample. With a time resolution of just a few microseconds, this approach is notably fast enough to study the domain motions that are typically associated with the activity of proteins but which have previously remained inaccessible. Here, crucial details are added to the characterization of the method. It is shown that single-particle reconstructions of apoferritin and Cowpea chlorotic mottle virus from revitrified samples are indistinguishable from those from conventional samples, demonstrating that melting and revitrification leaves the particles intact and that they do not undergo structural changes within the spatial resolution afforded by the instrument. How rapid revitrification affects the properties of the ice is also characterized, showing that revitrified samples exhibit comparable amounts of beam-induced motion. The results pave the way for microsecond time-resolved studies of the conformational dynamics of proteins and open up new avenues to study the vitrification process and to address beam-induced specimen movement.
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