Evidence map›Paper›PMID 40050283›Full record

ArticleNature communications2025

Energy filtering enables macromolecular MicroED data at sub-atomic resolution.

Max T B Clabbers, Johan Hattne, Michael W Martynowycz, Tamir Gonen

Erratum issuedAbstract 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. An erratum has been issued. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Membrane protein structure and dynamics probed by MicroED.Biochemical Society transactions · 2026
    Review
  6. Review
  7. Article
  8. Article
  9. Standards for MicroED.Acta crystallographica. Section C, Structural chemistry · 2025
    Article
  10. Article
  11. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Max T B ClabbersHoward Hughes Medical Institute, University of California, Los Angeles, CA, 90095, USA.ORCID http://orcid.org/0000-0002-5466-6508
Johan HattneHoward Hughes Medical Institute, University of California, Los Angeles, CA, 90095, USA.ORCID http://orcid.org/0000-0002-8936-0912
Michael W MartynowyczHoward Hughes Medical Institute, University of California, Los Angeles, CA, 90095, USA.
Tamir GonenHoward Hughes Medical Institute, University of California, Los Angeles, CA, 90095, USA. tgonen@g.ucla.edu.ORCID http://orcid.org/0000-0002-9254-4069

Funding

TRD4: Design and Engineering of MicroED hardware for nanocrystallization and time resolved studiesP41GM136508 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI GONEN, TAMIR · 2020 to 2024
$7.6M
Howard Hughes Medical Institute (HHMI) N/ANIGMS NIH HHS P41 GM136508United States Department of Defense | Defense Threat Reduction Agency (DTRA) HDTRA1-21-1-0004United States Department of Defense | Defense Threat Reduction Agency (DTRA) MCDC-2202-002U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) P41GM136508
6 · The paper itself

Abstract

High-resolution information is important for accurate structure modeling but is challenging to attain in macromolecular crystallography due to the rapid fading of diffracted intensities at increasing resolution. While direct electron detection essentially eliminates the read-out noise during MicroED data collection, other sources of noise remain and limit the measurement of faint high-resolution reflections. Inelastic scattering significantly contributes to noise, raising background levels and broadening diffraction peaks. We demonstrate a substantial improvement in signal-to-noise ratio by using energy filtering to remove inelastically scattered electrons. This strategy results in sub-atomic resolution MicroED data from proteinase K crystals, enabling the visualization of detailed structural features. Interestingly, reducing the noise further reveals diffuse scattering that may hold additional structural information. Our findings suggest that combining energy filtering and direct detection provides more accurate measurements at higher resolution, facilitating precise model refinement and improved insights into protein structure and function.

Indexed as

Macromolecular SubstancesCrystallography, X-RayElectronsEndopeptidase KModels, MolecularProtein ConformationSignal-To-Noise RatioEndopeptidase KMacromolecular Substances

Identifiers

PMID40050283
PMCPMC11885823

What OpenQuestion holds

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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.