ArticleStructural dynamics (Melville, N.Y.)2021
Microsecond melting and revitrification of cryo samples.
Article in Structural dynamics (Melville, N.Y.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 29 citations in OpenAlex.
- Cryo-EM sample preparation with soft-landing and laser flash melting.Nature communications · 2026Article
- Ultrathin liquid cells for microsecond time-resolved cryo-EM.Nature communications · 2026Article
- Determination of factors that allow cryogenic nanoscopy with high power illumination without devitrification.PloS one · 2026Article
- Laser flash melting cryo-EM samples to overcome preferred orientation.Nature methods · 2025Article
- Freeze frame: cracking molecular motion.Nature · 2025Article
- Review
- Shaped Laser Pulses for Microsecond Time-Resolved Cryo-EM: Outrunning Crystallization during Flash Melting.The journal of physical chemistry letters · 2024Article
- 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
- A simple flash and freeze system for cryogenic time-resolved electron microscopy.Frontiers in molecular biosciences · 2023Article
- Microsecond melting and revitrification of cryo samples: protein structure and beam-induced motion.Acta crystallographica. Section D, Structural biology · 2022Article
- Microsecond melting and revitrification of cryo samples with a correlative light-electron microscopy approach.Frontiers in molecular biosciences · 2022Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The dynamics of proteins that are associated with their function typically occur on the microsecond timescale, orders of magnitude faster than the time resolution of cryo-electron microscopy. We have recently introduced a novel approach to time-resolved cryo-electron microscopy that affords microsecond time resolution. It involves melting a cryo sample with a heating laser, so as to allow dynamics of the proteins to briefly occur in the liquid phase. When the laser is turned off, the sample rapidly revitrifies, trapping the particles in their transient configurations. Precise control of the temperature evolution of the sample is crucial for such an approach to succeed. Here, we provide a detailed characterization of the heat transfer occurring under laser irradiation as well as the associated phase behavior of the cryo sample. While areas close to the laser focus undergo melting and revitrification, surrounding regions crystallize.
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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.