Evidence map›Paper›PMID 23217682›Full record

ArticleStructure (London, England : 1993)2012

Protein secondary structure determination by constrained single-particle cryo-electron tomography.

Alberto Bartesaghi, Federico Lecumberry, Guillermo Sapiro, Sriram Subramaniam

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing 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

53 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. The big chill: Growth ofQRB discovery · 2024
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. High-resolution structure determination using high-throughput electron cryo-tomography.Acta crystallographica. Section D, Structural biology · 2022
    Review
  16. Article
  17. Article
  18. Review
  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

4 authors.

Alberto BartesaghiLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Federico Lecumberry
Guillermo Sapiro
Sriram Subramaniam

Funding

Technology Development for 3D Electron MicroscopyZIABC010826 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SUBRAMANIAM, SRIRAM · 2009 to 2019
$9.1M
Imaging cellular assemblies with three-dimensional electron microscopyZIABC010278 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SUBRAMANIAM, SRIRAM · 2009 to 2019
$8.0M
Intramural NIH HHS ZIA BC010278Intramural NIH HHS ZIA BC010826
6 · The paper itself

Abstract

Cryo-electron microscopy (cryo-EM) is a powerful technique for 3D structure determination of protein complexes by averaging information from individual molecular images. The resolutions that can be achieved with single-particle cryo-EM are frequently limited by inaccuracies in assigning molecular orientations based solely on 2D projection images. Tomographic data collection schemes, however, provide powerful constraints that can be used to more accurately determine molecular orientations necessary for 3D reconstruction. Here, we propose "constrained single-particle tomography" as a general strategy for 3D structure determination in cryo-EM. A key component of our approach is the effective use of images recorded in tilt series to extract high-resolution information and correct for the contrast transfer function. By incorporating geometric constraints into the refinement to improve orientational accuracy of images, we reduce model bias and overrefinement artifacts and demonstrate that protein structures can be determined at resolutions of ∼8 Å starting from low-dose tomographic tilt series.

Indexed as

Models, MolecularAlgorithmsChaperonin 60Cryoelectron MicroscopyElectron Microscope TomographyEscherichia coli ProteinsProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryRNA Polymerase IISaccharomyces cerevisiae ProteinsTranscription Factor TFIIBChaperonin 60Escherichia coli ProteinsRNA Polymerase IISaccharomyces cerevisiae ProteinsSUA7 protein, S cerevisiaeTranscription Factor TFIIB

Identifiers

PMID23217682
PMCPMC3600145

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.