Evidence map›Paper›PMID 39448878›Full record

ArticleNature methods2024

Elemental mapping in single-particle reconstructions by reconstructed electron energy-loss analysis.

Olivia Pfeil-Gardiner, Higor Vinícius Dias Rosa, Dietmar Riedel, Yu Seby Chen, Dominique Lörks, Pirmin Kükelhan, Martin Linck, Heiko Müller, Filip Van Petegem, Bonnie J Murphy

Abstract read
In one paragraph

Article in Nature methods, 2024. 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. Article
  3. Article
  4. Extending the reach of single-particle cryoEM.Current opinion in structural biology · 2025
    Review
  5. Article
  6. Review
  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

10 authors.

Olivia Pfeil-GardinerRedox and Metalloprotein Research Group, Max Planck Institute of Biophysics, Frankfurt, Germany.ORCID http://orcid.org/0000-0001-8095-0759
Higor Vinícius Dias RosaRedox and Metalloprotein Research Group, Max Planck Institute of Biophysics, Frankfurt, Germany.ORCID http://orcid.org/0000-0002-5743-4745
Dietmar RiedelFacility for Electron Microscopy, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.ORCID http://orcid.org/0000-0003-2970-6894
Yu Seby ChenThe University of British Columbia, Vancouver, British Columbia, Canada.ORCID http://orcid.org/0000-0002-0793-2391
Dominique LörksCEOS GmbH, Heidelberg, Germany.
Pirmin KükelhanCEOS GmbH, Heidelberg, Germany.
Martin LinckCEOS GmbH, Heidelberg, Germany.
Heiko MüllerCEOS GmbH, Heidelberg, Germany.
Filip Van PetegemThe University of British Columbia, Vancouver, British Columbia, Canada.
Bonnie J MurphyRedox and Metalloprotein Research Group, Max Planck Institute of Biophysics, Frankfurt, Germany. bonnie.murphy@biophys.mpg.de.ORCID http://orcid.org/0000-0001-6341-9368

Funding

EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council) 101116848
6 · The paper itself

Abstract

For macromolecular structures determined by cryogenic electron microscopy, no technique currently exists for mapping elements to defined locations, leading to errors in the assignment of metals and other ions, cofactors, substrates, inhibitors and lipids that play essential roles in activity and regulation. Elemental mapping in the electron microscope is well established for dose-tolerant samples but is challenging for biological samples, especially in a cryo-preserved state. Here we combine electron energy-loss spectroscopy with single-particle image processing to allow elemental mapping in cryo-preserved macromolecular complexes. Proof-of-principle data show that our method, reconstructed electron energy-loss (REEL) analysis, allows a three-dimensional reconstruction of electron energy-loss spectroscopy data, such that a high total electron dose is accumulated across many copies of a complex. Working with two test samples, we demonstrate that we can reliably localize abundant elements. We discuss the current limitations of the method and potential future developments.

Indexed as

Cryoelectron MicroscopySpectroscopy, Electron Energy-LossImage Processing, Computer-AssistedImaging, Three-DimensionalMacromolecular SubstancesSingle Molecule ImagingMacromolecular Substances

Identifiers

PMID39448878
PMCPMC11621030

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LicenceCC BY
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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.