Evidence map›Paper›PMID 31768058›Full record

ArticleNature methods2020

In situ structure determination at nanometer resolution using TYGRESS.

Kangkang Song, Zhiguo Shang, Xiaofeng Fu, Xiaochu Lou, Nikolaus Grigorieff, Daniela Nicastro

Abstract read
In one paragraph

Article in Nature methods, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Article
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  4. Cryo-EM single-particle analysis expanding towards increasingly native samples.Acta crystallographica. Section D, Structural biology · 2025
    Review
  5. Review
  6. Article
  7. Article
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  11. Structural determination and modeling of ciliary microtubules.Acta crystallographica. Section D, Structural biology · 2024
    Review
  12. The big chill: Growth ofQRB discovery · 2024
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
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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

6 authors.

Kangkang Song *Departments of Cell Biology and Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Zhiguo Shang *Departments of Cell Biology and Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Xiaofeng FuDepartments of Cell Biology and Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Xiaochu LouDepartments of Cell Biology and Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Nikolaus GrigorieffJanelia Farm Research Campus, Howard Hughes Medical Institute, Ashburn, VA, USA.
Daniela NicastroDepartments of Cell Biology and Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, USA. daniela.nicastro@utsouthwestern.edu.ORCID http://orcid.org/0000-0002-0122-7173

Funding

Structure and Function of Complexes that Regulate Ciliary MotilityR01GM083122 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI Daniela Nicastro · 2007 to 2026
$6.2M
Resolution Improvement for Cellular CryoEM to study Dynamic Assemblies in CellsR01GM111506 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI NICASTRO, DANIELA · 2014 to 2017
$1.4M
NIGMS NIH HHS R01 GM083122NIGMS NIH HHS R01 GM111506
6 · The paper itself

Abstract

The resolution of subtomogram averages calculated from cryo-electron tomograms (cryo-ET) of crowded cellular environments is often limited owing to signal loss in, and misalignment of, the subtomograms. By contrast, single-particle cryo-electron microscopy (SP-cryo-EM) routinely reaches near-atomic resolution of isolated complexes. We report a method called 'tomography-guided 3D reconstruction of subcellular structures' (TYGRESS) that is a hybrid of cryo-ET and SP-cryo-EM, and is able to achieve close-to-nanometer resolution of complexes inside crowded cellular environments. TYGRESS combines the advantages of SP-cryo-EM (images with good signal-to-noise ratio and contrast, as well as minimal radiation damage) and subtomogram averaging (three-dimensional alignment of macromolecules in a complex sample). Using TYGRESS, we determined the structure of the intact ciliary axoneme with up to resolution of 12 Å. These results reveal many structural details that were not visible by cryo-ET alone. TYGRESS is generally applicable to cellular complexes that are amenable to subtomogram averaging.

Indexed as

NanotechnologyCryoelectron MicroscopyImage Processing, Computer-AssistedMolecular StructureTetrahymena thermophila

Identifiers

PMID31768058
PMCPMC7004880

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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.