Evidence map›Paper›PMID 40744008›Full record

ArticleStructure (London, England : 1993)2025

Sub-3 Å resolution protein structure determination by single-particle cryo-EM at 100 keV.

Dimple Karia, Adrian F Koh, Wen Yang, Victoria I Cushing, Benjamin Basanta, Daniel B Mihaylov, Sagar Khavnekar, Ondřej Vyroubal, Miloš Malínský, Ondřej Sháněl and 7 more

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 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. Article
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  3. Review
  4. Review
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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

17 authors.

Dimple KariaMaterials and Structural Analysis Division, Thermo Fisher Scientific, Achtseweg Noord 5, 5651 Eindhoven, the Netherlands. Electronic address: dimple.karia@thermofisher.com.
Adrian F KohMaterials and Structural Analysis Division, Thermo Fisher Scientific, Achtseweg Noord 5, 5651 Eindhoven, the Netherlands. Electronic address: adrian.koh@thermofisher.com.
Wen YangMaterials and Structural Analysis Division, Thermo Fisher Scientific, Achtseweg Noord 5, 5651 Eindhoven, the Netherlands.
Victoria I CushingThe Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, London SW3 6JB, UK.
Benjamin BasantaDepartment of Integrative Structural and Computational Biology, Scripps Research, La Jolla, CA 92024, USA.
Daniel B MihaylovMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Sagar KhavnekarMax Planck Institute of Biochemistry, CryoEM Technology, Martinsried, Germany.
Ondřej VyroubalMaterials and Structural Analysis Division, Thermo Fisher Scientific, Achtseweg Noord 5, 5651 Eindhoven, the Netherlands.
Miloš MalínskýMaterials and Structural Analysis Division, Thermo Fisher Scientific, Achtseweg Noord 5, 5651 Eindhoven, the Netherlands.
Ondřej ShánělMaterials and Structural Analysis Division, Thermo Fisher Scientific, Achtseweg Noord 5, 5651 Eindhoven, the Netherlands.
Vojtěch DoležalMaterials and Structural Analysis Division, Thermo Fisher Scientific, Achtseweg Noord 5, 5651 Eindhoven, the Netherlands.
Jürgen PlitzkoMax Planck Institute of Biochemistry, CryoEM Technology, Martinsried, Germany.
Lingbo YuMaterials and Structural Analysis Division, Thermo Fisher Scientific, Achtseweg Noord 5, 5651 Eindhoven, the Netherlands. Electronic address: lingbo.yu@thermofisher.com.
Gabriel C LanderDepartment of Integrative Structural and Computational Biology, Scripps Research, La Jolla, CA 92024, USA.
A Radu AricescuMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Basil J GreberThe Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, London SW3 6JB, UK.
Abhay KotechaMaterials and Structural Analysis Division, Thermo Fisher Scientific, Achtseweg Noord 5, 5651 Eindhoven, the Netherlands. Electronic address: abhay.kotecha@stjude.org.

Funding

Automated, optimized, intelligent data collection for cryo-EMR01GM143805 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI LANDER, GABRIEL C · 2021 to 2025
$4.7M
NIGMS NIH HHS R01 GM143805
6 · The paper itself

Abstract

Cryoelectron microscopy (cryo-EM) has transformed structural biology by providing high-resolution insights into biological macromolecules. We report sub-3 Å resolution structures using the 100 keV Tundra cryo-TEM, equipped with the Falcon C direct electron detector (DED). This system combines advanced optics, extreme-brightness field emission gun (XFEG), and SP-TWIN lens to enhance coherence and resolution. The semi-automated loader reduced contamination and drift, enabling extended data collection, while the high detective quantum efficiency (DQE) of Falcon C improved signal-to-noise ratio. We validated performance by determining structures of biological samples, including apoferritin (2.1 Å), T20S proteasome (2.7 Å), GABA

Indexed as

Cryoelectron MicroscopySingle Molecule ImagingApoferritinsHumansModels, MolecularProteasome Endopeptidase ComplexProtein ConformationApoferritinsProteasome Endopeptidase Complex100 keV TEMAAV9 capsidcryo-EMDEDdirect electron detectorGABA(A) receptorhaemoglobinsingle particle analysisstructural biologyT20S proteasometransthyretin

Identifiers

PMID40744008
PMCPMC12372669

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.