Evidence map›Paper›PMID 40439681›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2025

High-Throughput MicroED for Probing Ion Channel Dynamics.

Marc J Gallenito, Max Tb Clabbers, Jieye Lin, Johan Hattne, Tamir Gonen

Abstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Membrane protein structure and dynamics probed by MicroED.Biochemical Society transactions · 2026
    Review
  2. Review
  3. Article
  4. High-Throughput MicroED for Probing Ion Channel Dynamics.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    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

5 authors.

Marc J GallenitoDepartment of Biological Chemistry, University of California, Los Angeles, CA, 90095, US.ORCID https://orcid.org/0000-0002-5096-724X
Max Tb ClabbersDepartment of Biological Chemistry, University of California, Los Angeles, CA, 90095, US.ORCID https://orcid.org/0000-0002-5466-6508
Jieye LinDepartment of Biological Chemistry, University of California, Los Angeles, CA, 90095, US.ORCID https://orcid.org/0009-0003-9008-5115
Johan HattneDepartment of Biological Chemistry, University of California, Los Angeles, CA, 90095, US.ORCID https://orcid.org/0000-0002-8936-0912
Tamir GonenDepartment of Biological Chemistry, University of California, Los Angeles, CA, 90095, US.ORCID https://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, NANNENGA, BRENT · 2020 to 2024
$7.6M
Defense Threat Reduction Agency HDTRA 1-21-0004Howard Hughes Medical InstituteNIGMS NIH HHS P41 GM136508NIH HHS P41GM136508U.S. Department of Defense MCDC-2202-002
6 · The paper itself

Abstract

Ion channels play a crucial role in ion transport and are integral to fundamental physiological processes. Understanding channel structures is essential for elucidating the mechanisms of ion permeation and selectivity beyond simple computational simulations. Visualizing dynamics at high resolution, however, remains a significant challenge by structural techniques. In this study, high-throughput microcrystal electron diffraction (MicroED) is applied to explore the structural dynamics of two ion channels, the non-selective ion channel NaK and its mutant, NaK2CNG. This approach utilizes automated data collection and processing to capture distinct structural substates from a large number of microcrystals, offering a deeper understanding of ion channel mechanisms. From a subset of NaK structures, consistent sodium binding at specific sites is observed. In contrast, NaK2CNG appears more dynamic and undergoes dilation of the selectivity filter upon potassium binding. Further, the conduction state of NaK2CNG appears to be influenced by channel gating. Comparative analysis of these structures suggests that plasticity of the selectivity filter may contribute to the non-selectivity of these channels, potentially allowing dynamic control over ion passage. These studies demonstrate the potential to employ high-throughput MicroED as a technique to address persistent questions regarding ion channel permeation, complementing current computational molecular dynamics studies.

Indexed as

Ion ChannelsIon Channel GatingMolecular Dynamics SimulationIon ChannelsIon Channelsion permeationion selectivitymembrane proteinsMicroEDstructural biology

Identifiers

PMID40439681
PMCPMC12376597

What OpenQuestion holds

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LicenceCC BY
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.