Evidence map›Paper›PMID 39231985›Full record

ArticleNature communications2024

Small LEA proteins mitigate air-water interface damage to fragile cryo-EM samples during plunge freezing.

Kaitlyn M Abe, Gan Li, Qixiang He, Timothy Grant, Ci Ji Lim

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
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  8. Review
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  13. Foam film vitrification for cryo-EM.Nature communications · 2025
    Article
  14. Article
  15. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Kaitlyn M AbeDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI, 53706, USA.ORCID http://orcid.org/0000-0001-6055-5604
Gan LiDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI, 53706, USA.
Qixiang HeDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI, 53706, USA.ORCID http://orcid.org/0000-0002-0738-679X
Timothy GrantDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI, 53706, USA.ORCID http://orcid.org/0000-0002-4855-8703
Ci Ji LimDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI, 53706, USA. ciji.lim@wisc.edu.ORCID http://orcid.org/0000-0003-3327-1926

Funding

Unraveling the Telomere Black Box: A New Single-Molecule Approach to Define the Telomere Chromatin Landscape and its Functional MechanismsDP2GM150023 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI LIM, CI JI · 2022 to 2025
$2.3M
Predoctoral Training in Molecular BiophysicsT32GM130550 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI SENES, ALESSANDRO · 2019 to 2023
$1.5M
Structural understanding of human shelterin complex assembly at telomere and its regulation mechanism of telomerase activityR00GM131023 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI LIM, CI JI · 2020 to 2022
$730k
NIGMS NIH HHS DP2 GM150023NIGMS NIH HHS R00 GM131023NIGMS NIH HHS T32 GM130550U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) DP2GM150023U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R00GM131023U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) T32GM130550
6 · The paper itself

Abstract

Air-water interface (AWI) interactions during cryo-electron microscopy (cryo-EM) sample preparation cause significant sample loss, hindering structural biology research. Organisms like nematodes and tardigrades produce Late Embryogenesis Abundant (LEA) proteins to withstand desiccation stress. Here we show that these LEA proteins, when used as additives during plunge freezing, effectively mitigate AWI damage to fragile multi-subunit molecular samples. The resulting high-resolution cryo-EM maps are comparable to or better than those obtained using existing AWI damage mitigation methods. Cryogenic electron tomography reveals that particles are localized at specific interfaces, suggesting LEA proteins form a barrier at the AWI. This interaction may explain the observed sample-dependent preferred orientation of particles. LEA proteins offer a simple, cost-effective, and adaptable approach for cryo-EM structural biologists to overcome AWI-related sample damage, potentially revitalizing challenging projects and advancing the field of structural biology.

Indexed as

AirCryoelectron MicroscopyFreezingWaterAnimalsElectron Microscope TomographyNematodaTardigradaWater

Identifiers

PMID39231985
PMCPMC11375022

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.