ArticleNature methods2025
Laser flash melting cryo-EM samples to overcome preferred orientation.
Article in Nature methods, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed.
- Control of ice thickness in cryo-EM via confinement.Nature methods · 2026Article
- Direct deposition on pre-cooled grids: a new approach to sub-millisecond cryoEM grid preparation.Acta crystallographica. Section D, Structural biology · 2026Article
- Integrating multitemperature sample preparation with particle rebalancing addresses preferred orientation.PNAS nexus · 2026Article
- Two datasets are better than one: method of double moments for 3D reconstruction in cryo-EM.Inverse problems · 2026Article
- Article
- prismPYP: Power-spectrum and image domain learning for self-supervised micrograph evaluation.Structure (London, England : 1993) · 2026Article
- CryoWriter: a robotic solution for improved Cryo-EM grid preparation.Nature communications · 2026Article
- Extending microsecond time-resolved cryo-electron microscopy with laser flash melting.Nature reviews. Molecular cell biology · 2026Article
- Ultrathin liquid cells for microsecond time-resolved cryo-EM.Nature communications · 2026Article
- Overcoming Preferred Orientation in Cryo-EM With Ultrasonic Excitation During Vitrification.bioRxiv : the preprint server for biology · 2025Article
- Laser-Induced Rehydration of Cryo-Landed Proteins Restores Native Structure.Molecular & cellular proteomics : MCP · 2025Article
- RNA-Protein Assemblies: A Review of Biophysical Principles and Coarse-Grained Modeling Approaches.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Sample preparation remains a bottleneck for protein structure determination by cryo-electron microscopy. A frequently encountered issue is that proteins adsorb to the air-water interface of the sample in a limited number of orientations. This makes it challenging to obtain high-resolution reconstructions, or may even cause projects to fail altogether. We have previously observed that laser flash melting and revitrification of cryo-EM samples reduces preferred orientation for large, symmetric particles. Here we demonstrate that our method can in fact be used to scramble the orientation of proteins of a range of sizes and symmetries. The effect can be enhanced for some proteins by increasing the heating rate during flash melting or by depositing amorphous ice onto the sample prior to revitrification. This also allows us to shed light onto the underlying mechanism. Our experiments establish a set of tools for overcoming preferred orientation that can be easily integrated into existing workflows.
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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.