Evidence map›Paper›PMID 40365900›Full record

ArticleFaraday discussions2025

Cryo-EM for atomic characterization of supramolecular gels.

Ravi R Sonani, Simona Bianco, Mark A B Kreutzberger, Dave J Adams, Edward H Egelman

Abstract read
In one paragraph

Article in Faraday discussions, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

  1. Light-triggered modulation in donor-acceptor dipeptide assemblies.Chemical communications (Cambridge, England) · 2026
    Article
  2. Article
  3. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Ravi R SonaniDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22903, USA. egelman@virginia.edu.ORCID http://orcid.org/0000-0002-6212-2869
Simona BiancoSchool of Chemistry, University of Glasgow, Glasgow, G12 8QQ, UK.ORCID http://orcid.org/0000-0001-5305-8546
Mark A B KreutzbergerDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22903, USA. egelman@virginia.edu.ORCID http://orcid.org/0000-0002-1269-2089
Dave J AdamsSchool of Chemistry, University of Glasgow, Glasgow, G12 8QQ, UK.ORCID http://orcid.org/0000-0002-3176-1350
Edward H EgelmanDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22903, USA. egelman@virginia.edu.ORCID http://orcid.org/0000-0003-4844-5212

Funding

Cryo-EM of Helical Protein and Nucleoprotein Polymers at Near Atomic ResolutionR35GM122510 · NIGMS · UNIVERSITY OF VIRGINIA · PI EDWARD H. EGELMAN · 2017 to 2026
$7.3M
UVA molecular electron microscopy core for the Mid-Atlantic regionU24GM116790 · NIGMS · UNIVERSITY OF VIRGINIA · PI GALKIN, VITOLD, SAMSO, MONTSERRAT · 2017 to 2021
$2.9M
Molecular Electron Microscopy Core Facility ImprovementsG20RR031199 · NCRR · UNIVERSITY OF VIRGINIA · PI SHUPNIK, MARGARET A · 2010 to 2010
$2.0M
300 keV Liquid Helium Robotic MicroscopeS10RR025067 · NCRR · UNIVERSITY OF VIRGINIA · PI EGELMAN, EDWARD H. · 2009 to 2009
$2.0M
NCRR NIH HHS G20 RR031199NCRR NIH HHS S10 RR025067NIGMS NIH HHS R35 GM122510NIGMS NIH HHS U24 GM116790
6 · The paper itself

Abstract

While there have been great advances in the design and synthesis of supramolecular gels, their characterization methods have largely stayed the same, with electron microscopy of dried samples, or small-angle scattering and spectroscopy dominating the approaches used. Although these methods provide valuable insights into structural properties, they are unable to unambiguously generate reliable atomic models that can further guide the site-specific modification of supramolecular gelators. Cryogenic electron microscopy (cryo-EM), allowing the high-resolution imaging of the sample in a hydrated state, has emerged as the dominant technique in structural biology, but has yet to become a routine method in materials science. Here, we describe the use of cryo-EM to determine the atomic structure of the tubular micelle formed by the dipeptide CarbIF, revealing the mechanism of assembly and gelation. Using the CarbIF micelle as an example, we highlight some of the challenges in using cryo-EM to study such materials, and how determination of the helical symmetry can be the most difficult aspect of such a project.

Identifiers

PMID40365900
PMCPMC12076579

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Registered trials

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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.