Evidence map›Paper›PMID 31080120›Full record

ArticleStructure (London, England : 1993)2019

Fusion of DARPin to Aldolase Enables Visualization of Small Protein by Cryo-EM.

Qing Yao, Sara J Weaver, Jee-Young Mock, Grant J Jensen

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. Review
  2. Hidden gems bring proteins into view.Nature chemical biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Cryo-electron microscopy-based drug design.Frontiers in molecular biosciences · 2024
    Review
  10. Cryo-EM structure determination of small therapeutic protein targets at 3 Å-resolution using a rigid imaging scaffold.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Review
  12. Structural conservation among variants of the SARS-CoV-2 spike postfusion bundle.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Cryo-EM structure determination of small proteins by nanobody-binding scaffolds (Legobodies).Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  18. Generation of ordered protein assemblies using rigid three-body fusion.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Review
  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.

Qing YaoDivision of Biology and Biological Engineering, California Institute of Technology, 1200 E. California Boulevard, Pasadena, CA 91125, USA.
Sara J WeaverDivision of Chemistry and Chemical Engineering, California Institute of Technology, 1200 E. California Boulevard, Pasadena, CA 91125, USA.
Jee-Young MockDivision of Chemistry and Chemical Engineering, California Institute of Technology, 1200 E. California Boulevard, Pasadena, CA 91125, USA.
Grant J JensenDivision of Biology and Biological Engineering, California Institute of Technology, 1200 E. California Boulevard, Pasadena, CA 91125, USA; Howard Hughes Medical Institute, 1200 E. California Boulevard, Pasadena, CA 91125, USA. Electronic address: jensen@caltech.edu.

Funding

X-ray Cryst. CoreP50GM082545 · NIGMS · UNIVERSITY OF UTAH · PI SUNDQUIST, WESLEY I. · 2007 to 2018
$51.1M
Howard Hughes Medical InstituteNIGMS NIH HHS P50 GM082545
6 · The paper itself

Abstract

Solving protein structures by single-particle cryoelectron microscopy (cryo-EM) has become a crucial tool in structural biology. While exciting progress is being made toward the visualization of small macromolecules, the median protein size in both eukaryotes and bacteria is still beyond the reach of cryo-EM. To overcome this problem, we implemented a platform strategy in which a small protein target was rigidly attached to a large, symmetric base via a selectable adapter. Of our seven designs, the best construct used a designed ankyrin repeat protein (DARPin) rigidly fused to tetrameric rabbit muscle aldolase through a helical linker. The DARPin retained its ability to bind its target: GFP. We solved the structure of this complex to 3.0 Å resolution overall, with 5-8 Å resolution in the GFP region. As flexibility in the DARPin position limited the overall resolution of the target, we describe strategies to rigidify this element.

Indexed as

Animalsbeta-GalactosidaseBinding SitesCloning, MolecularCryoelectron MicroscopyEscherichia coliFructose-Bisphosphate AldolaseGene ExpressionGenetic VectorsGreen Fluorescent ProteinsHumansModels, MolecularMuscle ProteinsProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-Strandbeta-GalactosidaseFructose-Bisphosphate AldolaseGreen Fluorescent ProteinsMuscle ProteinsRecombinant Fusion ProteinsRecombinant ProteinsSingle-Chain Antibodiesaldolaseartificial proteincryo-electron microscopyCryoEMDARPinElectron cryo-microscopyplatformprotein designSingle-particle analysis

Identifiers

PMID31080120
PMCPMC6610650

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.