Evidence map›Paper›PMID 27821763›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Design of a molecular support for cryo-EM structure determination.

Thomas G Martin, Tanmay A M Bharat, Andreas C Joerger, Xiao-Chen Bai, Florian Praetorius, Alan R Fersht, Hendrik Dietz, Sjors H W Scheres

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed.

  1. DNA-Guided Robust Single-Protein Electronic Readout.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Review
  3. Article
  4. DNA origami: a tool to evaluate and harness transcription factors.Journal of molecular medicine (Berlin, Germany) · 2023
    Review
  5. 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
  6. Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. DNA origami nano-mechanics.Chemical Society reviews · 2021
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Nuclease resistance of DNA nanostructures.Nature reviews. Chemistry · 2021
    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

8 authors.

Thomas G MartinMedical Research Council Laboratory of Molecular Biology, Cambridge Biomedical Campus, Cambridge CB2 0QH, United Kingdom.
Tanmay A M BharatMedical Research Council Laboratory of Molecular Biology, Cambridge Biomedical Campus, Cambridge CB2 0QH, United Kingdom.
Andreas C JoergerMedical Research Council Laboratory of Molecular Biology, Cambridge Biomedical Campus, Cambridge CB2 0QH, United Kingdom.
Xiao-Chen BaiMedical Research Council Laboratory of Molecular Biology, Cambridge Biomedical Campus, Cambridge CB2 0QH, United Kingdom.
Florian PraetoriusPhysik Department, Walter Schottky Institute, Technische Universität München, 85748 Garching near Munich, Germany.
Alan R FershtMedical Research Council Laboratory of Molecular Biology, Cambridge Biomedical Campus, Cambridge CB2 0QH, United Kingdom.
Hendrik DietzPhysik Department, Walter Schottky Institute, Technische Universität München, 85748 Garching near Munich, Germany scheres@mrc-lmb.cam.ac.uk dietz@tum.de.
Sjors H W ScheresMedical Research Council Laboratory of Molecular Biology, Cambridge Biomedical Campus, Cambridge CB2 0QH, United Kingdom; scheres@mrc-lmb.cam.ac.uk dietz@tum.de.ORCID 0000-0002-0462-6540

Funding

European Research Council 256270Medical Research Council MC_EX_G0901534Medical Research Council MC_UP_A024_1010Medical Research Council MC_UP_A025_1013
6 · The paper itself

Abstract

Despite the recent rapid progress in cryo-electron microscopy (cryo-EM), there still exist ample opportunities for improvement in sample preparation. Macromolecular complexes may disassociate or adopt nonrandom orientations against the extended air-water interface that exists for a short time before the sample is frozen. We designed a hollow support structure using 3D DNA origami to protect complexes from the detrimental effects of cryo-EM sample preparation. For a first proof-of-principle, we concentrated on the transcription factor p53, which binds to specific DNA sequences on double-stranded DNA. The support structures spontaneously form monolayers of preoriented particles in a thin film of water, and offer advantages in particle picking and sorting. By controlling the position of the binding sequence on a single helix that spans the hollow support structure, we also sought to control the orientation of individual p53 complexes. Although the latter did not yet yield the desired results, the support structures did provide partial information about the relative orientations of individual p53 complexes. We used this information to calculate a tomographic 3D reconstruction, and refined this structure to a final resolution of ∼15 Å. This structure settles an ongoing debate about the symmetry of the p53 tetramer bound to DNA.

Indexed as

Cryoelectron MicroscopyDNAHumansImaging, Three-DimensionalMacromolecular SubstancesProtein ConformationProtein MultimerizationTumor Suppressor Protein p53WaterDNAMacromolecular SubstancesTP53 protein, humanTumor Suppressor Protein p53Watercryo-EMDNA-origamip53single particle analysisstructural biology

Identifiers

PMID27821763
PMCPMC5127339

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.