Evidence map›Paper›PMID 35191473›Full record

ArticleBiochemical Society transactions2022

Studying membrane proteins with MicroED.

Marc J Gallenito, Tamir Gonen

Abstract read
In one paragraph

Article in Biochemical Society transactions, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Unraveling atomic complexity from frozen samples.Structural dynamics (Melville, N.Y.) · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. MicroED Structure of a Protoglobin Reactive Carbene Intermediate.Journal of the American Chemical Society · 2023
    Article
  10. Review
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

2 authors.

Marc J GallenitoDepartment of Biological Chemistry, University of California, Los Angeles, Los Angeles CA 90095, U.S.A.
Tamir GonenDepartment of Biological Chemistry, University of California, Los Angeles, Los Angeles CA 90095, U.S.A.ORCID 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
NIGMS NIH HHS P41 GM136508
6 · The paper itself

Abstract

The structural investigation of biological macromolecules is indispensable in understanding the molecular mechanisms underlying diseases. Several structural biology techniques have been introduced to unravel the structural facets of biomolecules. Among these, the electron cryomicroscopy (cryo-EM) method microcrystal electron diffraction (MicroED) has produced atomic resolution structures of important biological and small molecules. Since its inception in 2013, MicroED established a demonstrated ability for solving structures of difficult samples using vanishingly small crystals. However, membrane proteins remain the next big frontier for MicroED. The intrinsic properties of membrane proteins necessitate improved sample handling and imaging techniques to be developed and optimized for MicroED. Here, we summarize the milestones of electron crystallography of two-dimensional crystals leading to MicroED of three-dimensional crystals. Then, we focus on four different membrane protein families and discuss representatives from each family solved by MicroED.

Indexed as

ElectronsMembrane ProteinsCryoelectron MicroscopyCrystallography, X-RayModels, MolecularMembrane Proteinscryo-EMmicrocrystal electron diffractionMicroEDtransmembrane proteins

Identifiers

PMID35191473
PMCPMC9022970

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.