Evidence map›Paper›PMID 27806259›Full record

ArticleStructure (London, England : 1993)2016

Antibody-Based Affinity Cryoelectron Microscopy at 2.6-Å Resolution.

Guimei Yu, Kunpeng Li, Pengwei Huang, Xi Jiang, Wen Jiang

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Developing Graphene Grids for Cryoelectron Microscopy.Frontiers in molecular biosciences · 2022
    Review
  8. High resolution single particle Cryo-EM refinement using JSPR.Progress in biophysics and molecular biology · 2021
    Review
  9. From Tube to Structure: SPA Cryo-EM Workflow Using Apoferritin as an Example.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  10. Article
  11. Structural Biology in the Multi-Omics Era.Journal of chemical information and modeling · 2020
    Article
  12. Article
  13. Structural Variability in the RLR-MAVS Pathway and Sensitive Detection of Viral RNAs.Medicinal chemistry (Shariqah (United Arab Emirates)) · 2019
    Review
  14. Article
  15. Biological Applications at the Cutting Edge of Cryo-Electron Microscopy.Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada · 2018
    Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. Cryo-EM: beyond the microscope.Current opinion in structural biology · 2017
    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

5 authors.

Guimei YuDepartment of Biological Science, Markey Center for Structural Biology, Purdue University, West Lafayette, IN 47907, USA.
Kunpeng LiDepartment of Biological Science, Markey Center for Structural Biology, Purdue University, West Lafayette, IN 47907, USA.
Pengwei HuangDivisions of Infectious Diseases, Cincinnati Children's Hospital Medical Center, Cincinnati, OH 45229, USA; Department of Pediatrics, University of Cincinnati College of Medicine, Cincinnati, OH 45267, USA.
Xi JiangDivisions of Infectious Diseases, Cincinnati Children's Hospital Medical Center, Cincinnati, OH 45229, USA; Department of Pediatrics, University of Cincinnati College of Medicine, Cincinnati, OH 45267, USA.
Wen JiangDepartment of Biological Science, Markey Center for Structural Biology, Purdue University, West Lafayette, IN 47907, USA. Electronic address: jiang12@purdue.edu.

Funding

HBGA receptors in host cell entry and infection of norovirusR01AI111095 · NIAID · PURDUE UNIVERSITY · PI JIANG, WEN, JIANG, XI · 2015 to 2019
$2.5M
Human monoclonal antibodies against norovirus.R21AI122132 · NIAID · CINCINNATI CHILDRENS HOSP MED CTR · PI JIANG, XI · 2016 to 2017
$429k
NIAID NIH HHS R01 AI111095NIAID NIH HHS R21 AI122132
6 · The paper itself

Abstract

The affinity cryoelectron microscopy (cryo-EM) approach has been explored in recent years to simplify and/or improve the sample preparation for cryo-EM, which can bring previously challenging specimens such as those of low abundance and/or unpurified ones within reach of the cryo-EM technique. Despite the demonstrated successes for solving structures to low to intermediate resolutions, the lack of near-atomic structures using this approach has led to a common perception of affinity cryo-EM as a niche technique incapable of reaching high resolutions. Here, we report a ∼2.6-Å structure solved using the antibody-based affinity grid approach with low-concentration Tulane virus purified from a low-yield cell-culture system that has been challenging to standard cryo-EM grid preparation. Quantitative analyses of the structure indicate data and reconstruction quality comparable with the conventional grid preparation method using samples at high concentration.

Indexed as

AntibodiesCryoelectron MicroscopyModels, MolecularMolecular StructureVirusesAntibodiesaffinity cryoelectron microscopyantibody-based affinity gridsingle-particle 3D reconstructionTulane virus

Identifiers

PMID27806259
PMCPMC5123806

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.