ReviewBiophysics reports2017
Opinion: hazards faced by macromolecules when confined to thin aqueous films.
Review in Biophysics reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
95 citing papers in PubMed.
- Cryo-EM sample preparation with soft-landing and laser flash melting.Nature communications · 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
- CryoWriter: a robotic solution for improved Cryo-EM grid preparation.Nature communications · 2026Article
- DM: a simple solution to suppress air-water interface interactions in cryo-EM.bioRxiv : the preprint server for biology · 2026Article
- A Surfactant Cocktail Overcomes Air-Water Interface Artifacts in Single-Particle CryoEM.bioRxiv : the preprint server for biology · 2026Article
- Direct Measurement of Protein Pair Interaction Potential.ACS nano · 2026Article
- Overcoming Preferred Orientation in Cryo-EM With Ultrasonic Excitation During Vitrification.bioRxiv : the preprint server for biology · 2025Article
- Laser flash melting cryo-EM samples to overcome preferred orientation.Nature methods · 2025Article
- Electrospray-based sample preparation for high-resolution protein structure elucidation by cryo-EM.Clinical and translational medicine · 2025Article
- Laser-Induced Rehydration of Cryo-Landed Proteins Restores Native Structure.Molecular & cellular proteomics : MCP · 2025Article
- CryoPROS: Correcting misalignment caused by preferred orientation using AI-generated auxiliary particles.Nature communications · 2025Article
- RNA sample optimization for cryo-EM analysis.Nature protocols · 2025Review
- Preparation of oxygen-sensitive proteins for high-resolution cryoEM structure determination using blot-free vitrification.Nature communications · 2025Article
- Structure of dimerized assimilatory NADPH-dependent sulfite reductase reveals the minimal interface for diflavin reductase binding.Nature communications · 2025Article
- Deconvolution to restore cryo-EM maps with anisotropic resolution.Research square · 2025Article
- Deconvolution to restore cryo-EM maps with anisotropic resolution.bioRxiv : the preprint server for biology · 2025Article
- Cryo-electron tomography pipeline for plasma membranes.Nature communications · 2025Article
- Structure of dimerized assimilatory NADPH-dependent sulfite reductase reveals the minimal interface for diflavin reductase binding.bioRxiv : the preprint server for biology · 2025Article
- Small LEA proteins mitigate air-water interface damage to fragile cryo-EM samples during plunge freezing.Nature communications · 2024Article
35 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Samples prepared for single-particle electron cryo-microscopy (cryo-EM) necessarily have a very high surface-to-volume ratio during the short period of time between thinning and vitrification. During this time, there is an obvious risk that macromolecules of interest may adsorb to the air-water interface with a preferred orientation, or that they may even become partially or fully unfolded at the interface. In addition, adsorption of macromolecules to an air-water interface may occur even before thinning. This paper addresses the question whether currently used methods of sample preparation might be improved if one could avoid such interfacial interactions. One possible way to do so might be to preemptively form a surfactant monolayer over the air-water interfaces, to serve as a structure-friendly slide and coverslip. An alternative is to immobilize particles of interest by binding them to some type of support film, which-to continue using the analogy-thus serves as a slide. In this case, the goal is not only to prevent the particles of interest from diffusing into contact with the air-water interface but also to increase the number of particles seen in each image. In this direction, it is natural to think of developing various types of affinity grids as structure-friendly alternatives to thin carbon films. Perhaps ironically, if precautions are not taken against adsorption of particles to air-water interfaces, sacrificial monolayers of denatured protein may take the roles of slide, coverslip, or even both.
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What OpenQuestion holds
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.