Evidence map›Paper›PMID 34709401›Full record

ReviewBiochemical Society transactions2021

Conquer by cryo-EM without physically dividing.

Gabriel C Lander, Robert M Glaeser

Abstract readReview
In one paragraph

Review in Biochemical Society transactions, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Unraveling atomic complexity from frozen samples.Structural dynamics (Melville, N.Y.) · 2025
    Article
  8. Article
  9. Structure of the lens MP20 mediated adhesive junction.bioRxiv : the preprint server for biology · 2024
    Article
  10. Cryo-EM sample preparation for high-resolution structure studies.Acta crystallographica. Section F, Structural biology communications · 2024
    Article
  11. Article
  12. Article
  13. Review
  14. 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

2 authors.

Gabriel C LanderDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, U.S.A.
Robert M GlaeserDivision of Molecular Biophysics and Integrative Bioimaging, Lawrence Berkeley National Laboratory, University of California, Berkeley, CA 94720, U.S.A.ORCID 0000-0003-1955-1825

Funding

Development of Laser-Based Phase Contrast for Biological Electron MicroscopyR01GM126011 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI MUELLER, HOLGER · 2017 to 2024
$3.9M
Extending the limits of cryo-EM to better understand TTR misfolding and aggregationR21AG067594 · NIA · SCRIPPS RESEARCH INSTITUTE, THE · PI LANDER, GABRIEL C · 2020 to 2021
$488k
Development of a pipeline for parallel elucidation of protein structuresR21GM142196 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI LANDER, GABRIEL C · 2021 to 2022
$488k
NIA NIH HHS R21 AG067594NIGMS NIH HHS R01 GM126011NIGMS NIH HHS R21 GM142196
6 · The paper itself

Abstract

This mini-review provides an update regarding the substantial progress that has been made in using single-particle cryo-EM to obtain high-resolution structures for proteins and other macromolecules whose particle sizes are smaller than 100 kDa. We point out that establishing the limits of what can be accomplished, both in terms of particle size and attainable resolution, serves as a guide for what might be expected when attempting to improve the resolution of small flexible portions of a larger structure using focused refinement approaches. These approaches, which involve computationally ignoring all but a specific, targeted region of interest on the macromolecules, is known as 'masking and refining,' and it thus is the computational equivalent of the 'divide and conquer' approach that has been used so successfully in X-ray crystallography. The benefit of masked refinement, however, is that one is able to determine structures in their native architectural context, without physically separating them from the biological connections that they require for their function. This mini-review also compares where experimental achievements currently stand relative to various theoretical estimates for the smallest particle size that can be successfully reconstructed to high resolution. Since it is clear that a substantial gap still remains between the two, we briefly recap the areas in which further improvement seems possible, both in equipment and in methods.

Indexed as

Cryoelectron MicroscopyCrystallography, X-RayMacromolecular SubstancesModels, MolecularMacromolecular Substancescryo-electron microscopydivide and conquerstructure determination

Identifiers

PMID34709401
PMCPMC9416522

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.