Evidence map›Paper›PMID 39955301›Full record

ArticleNature communications2025

A structural biology compatible file format for atomic force microscopy.

Yining Jiang, Zhaokun Wang, Simon Scheuring

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Review
  2. Automating Model Building for SPM Images of Biomolecules Using MISO.Journal of chemical information and modeling · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
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

3 authors.

Yining JiangBiochemistry & Structural Biology, Cell & Developmental Biology, and Molecular Biology (BCMB) Program, Weill Cornell Graduate School of Medical Sciences, New York, NY, USA.ORCID http://orcid.org/0000-0002-7624-4488
Zhaokun WangWeill Cornell Medicine, Department of Anesthesiology, New York, NY, USA.
Simon ScheuringWeill Cornell Medicine, Department of Anesthesiology, New York, NY, USA. sis2019@med.cornell.edu.ORCID http://orcid.org/0000-0003-3534-069X

Funding

Enabling physical stimuli in the study of structural dynamics: The sensory ion channelsDP1AT010874 · NCCIH · WEILL MEDICAL COLL OF CORNELL UNIV · PI SCHEURING, SIMON · 2019 to 2023
$5.9M
High-speed atomic force microscopy with microsecond time resolution for the study of channels and transportersR01NS110790 · NINDS · WEILL MEDICAL COLL OF CORNELL UNIV · PI Simon Scheuring · 2019 to 2026
$2.4M
NCCIH NIH HHS DP1 AT010874NINDS NIH HHS R01 NS110790U.S. Department of Health & Human Services | NIH | National Center for Complementary and Integrative Health (NCCIH) DP1AT010874U.S. Department of Health & Human Services | NIH | National Institute of Neurological Disorders and Stroke (NINDS) R01NS110790
6 · The paper itself

Abstract

Cryogenic electron microscopy (cryo-EM), X-ray crystallography, and nuclear magnetic resonance (NMR) contribute structural data that are interchangeable, cross-verifiable, and visualizable on common platforms, making them powerful tools for our understanding of protein structures. Unfortunately, atomic force microscopy (AFM) has so far failed to interface with these structural biology methods, despite the recent development of localization AFM (LAFM) that allows extracting high-resolution structural information from AFM data. Here, we build on LAFM and develop a pipeline that transforms AFM data into 3D-density files (.afm) that are readable by programs commonly used to visualize, analyze, and interpret structural data. We show that 3D-LAFM densities can serve as force fields to steer molecular dynamics flexible fitting (MDFF) to obtain structural models of previously unresolved states based on AFM observations in close-to-native environment. Besides, the .afm format enables direct 3D or 2D visualization and analysis of conventional AFM images. We anticipate that the file format will find wide usage and embed AFM in the repertoire of methods routinely used by the structural biology community, allowing AFM researchers to deposit data in repositories in a format that allows comparison and cross-verification with data from other techniques.

Indexed as

Microscopy, Atomic ForceProteinsCryoelectron MicroscopyCrystallography, X-RayMolecular Dynamics SimulationProtein ConformationSoftwareProteins

Identifiers

PMID39955301
PMCPMC11829953

What OpenQuestion holds

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LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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.