Evidence map›Paper›PMID 32647824›Full record

ArticleJournal of structural biology: X2020

Sub-2 Angstrom resolution structure determination using single-particle cryo-EM at 200 keV.

Mengyu Wu, Gabriel C Lander, Mark A Herzik

Abstract read
In one paragraph

Article in Journal of structural biology: X, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing 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

46 citing papers in PubMed.

  1. Article
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  3. Article
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  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. CryoEM Workflow Acceleration with Feret Signatures.International journal of molecular sciences · 2024
    Article
  15. Article
  16. Structural Analysis of Protein Complexes by Cryo-Electron Microscopy.Methods in molecular biology (Clifton, N.J.) · 2024
    Review
  17. Cryo-electron microscopy-based drug design.Frontiers in molecular biosciences · 2024
    Review
  18. Article
  19. Near-atomic resolution reconstructions from in situ revitrified cryo samples.Acta crystallographica. Section D, Structural biology · 2023
    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

3 authors.

Mengyu WuDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, United States.
Gabriel C LanderDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, United States.
Mark A HerzikDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093, United States.

Funding

Molecular basis of axonal transport described by high-resolution 3D imagingDP2EB020402 · NIBIB · SCRIPPS RESEARCH INSTITUTE, THE · PI LANDER, GABRIEL C · 2014 to 2014
$2.8M
COMPUTING AND DATA STORAGE CLUSTER FOR ELECTRON MICROSCOPYS10OD021634 · OD · SCRIPPS RESEARCH INSTITUTE, THE · PI LANDER, GABRIEL C · 2016 to 2016
$531k
Conformational ensembles associated with TRPV3 gatingR21AR072910 · NIAMS · SCRIPPS RESEARCH INSTITUTE, THE · PI LANDER, GABRIEL C · 2018 to 2019
$467k
NIAMS NIH HHS R21 AR072910NIBIB NIH HHS DP2 EB020402NIH HHS S10 OD021634
6 · The paper itself

Abstract

Although the advent of direct electron detectors (DEDs) and software developments have enabled the routine use of single-particle cryogenic electron microscopy (cryo-EM) for structure determination of well-behaved specimens to high-resolution, there nonetheless remains a discrepancy between the resolutions attained for biological specimens and the information limits of modern transmission electron microscopes (TEMs). Instruments operating at 300 kV equipped with DEDs are the current paradigm for high-resolution single-particle cryo-EM, while 200 kV TEMs remain comparatively underutilized for purposes beyond sample screening. Here, we expand upon our prior work and demonstrate that one such 200 kV microscope, the Talos Arctica, equipped with a K2 DED is capable of determining structures of macromolecules to as high as ∼1.7 Å resolution. At this resolution, ordered water molecules are readily assigned and holes in aromatic residues can be clearly distinguished in the reconstructions. This work emphasizes the utility of 200 kV electrons for high-resolution single-particle cryo-EM and applications such as structure-based drug design.

Indexed as

200 keVCryo-EMElectron microscopyMicroscope aberrationsSingle particle cryo-EMTwo-condenser lens

Identifiers

PMID32647824
PMCPMC7337053

What OpenQuestion holds

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Registered trials

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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.