Evidence map›Paper›PMID 33293416›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

MicroED structure of lipid-embedded mammalian mitochondrial voltage-dependent anion channel.

Michael W Martynowycz, Farha Khan, Johan Hattne, Jeff Abramson, Tamir Gonen

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.9field-weighted citation impact, top 8% of its field
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

33 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Membrane protein structure and dynamics probed by MicroED.Biochemical Society transactions · 2026
    Review
  3. Review
  4. Review
  5. Unraveling atomic complexity from frozen samples.Structural dynamics (Melville, N.Y.) · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. MicroED Structure of a Protoglobin Reactive Carbene Intermediate.Journal of the American Chemical Society · 2023
    Article
  13. MicroED in drug discovery.Current opinion in structural biology · 2023
    Review
  14. Design and implementation of suspended drop crystallization.bioRxiv : the preprint server for biology · 2023
    Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. 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 at 2 institutions in 1 country.

Michael W MartynowyczHoward Hughes Medical Institute, University of California, Los Angeles, CA 90095.
Farha KhanDepartment of Physiology, University of California, Los Angeles, CA 90095.
Johan HattneHoward Hughes Medical Institute, University of California, Los Angeles, CA 90095.ORCID 0000-0002-8936-0912
Jeff AbramsonDepartment of Physiology, University of California, Los Angeles, CA 90095.
Tamir GonenHoward Hughes Medical Institute, University of California, Los Angeles, CA 90095; tgonen@g.ucla.edu.ORCID 0000-0002-9254-4069
Howard Hughes Medical Institute · USUniversity of California, Los Angeles · US

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
Deciphering molecular details of cellular sugar transport and their roles in diseaseR35GM135175 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI ABRAMSON, JEFFREY S · 2020 to 2024
$3.9M
Howard Hughes Medical InstituteNIGMS NIH HHS P41 GM136508NIGMS NIH HHS R35 GM135175
6 · The paper itself

Abstract

A structure of the murine voltage-dependent anion channel (VDAC) was determined by microcrystal electron diffraction (MicroED). Microcrystals of an essential mutant of VDAC grew in a viscous bicelle suspension, making it unsuitable for conventional X-ray crystallography. Thin, plate-like crystals were identified using scanning-electron microscopy (SEM). Crystals were milled into thin lamellae using a focused-ion beam (FIB). MicroED data were collected from three crystal lamellae and merged for completeness. The refined structure revealed unmodeled densities between protein monomers, indicative of lipids that likely mediate contacts between the proteins in the crystal. This body of work demonstrates the effectiveness of milling membrane protein microcrystals grown in viscous media using a focused ion beam for subsequent structure determination by MicroED. This approach is well suited for samples that are intractable by X-ray crystallography. To our knowledge, the presented structure is a previously undescribed mutant of the membrane protein VDAC, crystallized in a lipid bicelle matrix and solved by MicroED.

Indexed as

AnimalsCryoelectron MicroscopyCrystallizationLipidsMiceMicroscopy, Electron, ScanningMicroscopy, Electron, TransmissionMitochondrial ProteinsProtein ConformationVoltage-Dependent Anion ChannelsLipidsMitochondrial ProteinsVoltage-Dependent Anion Channelsbicelle crystallizationcryoEMFIB/SEMmicrocrystal electron diffractionMicroED

Identifiers

PMID33293416
PMCPMC7768720
OpenAlexW3112145719

What OpenQuestion holds

Textmetadata
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.