Evidence map›Paper›PMID 28068317›Full record

ArticleNature methods2017

Cryogenic optical localization provides 3D protein structure data with Angstrom resolution.

Siegfried Weisenburger, Daniel Boening, Benjamin Schomburg, Karin Giller, Stefan Becker, Christian Griesinger, Vahid Sandoghdar

Abstract read
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In one paragraph

Article in Nature methods, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing 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

46 citing papers in PubMed.

  1. Article
  2. Thousandfold Expansion Microscopy.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Cryogenic light microscopy of vitrified samples with angstrom precision.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Review
  6. Single-Molecule 3D Nanoscopy for Application to Cryofixed Samples.The journal of physical chemistry. B · 2025
    Article
  7. Time-deterministic cryo-optical microscopy.Light, science & applications · 2025
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Higher-order transient membrane protein structures.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Review
  16. Future Paths in Cryogenic Single-Molecule Fluorescence Spectroscopy.The journal of physical chemistry. C, Nanomaterials and interfaces · 2024
    Review
  17. Review
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Siegfried WeisenburgerMax Planck Institute for the Science of Light, Erlangen, Germany.ORCID 0000-0003-2044-0372
Daniel BoeningMax Planck Institute for the Science of Light, Erlangen, Germany.
Benjamin SchomburgMax Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Karin GillerMax Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Stefan BeckerMax Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Christian GriesingerMax Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Vahid SandoghdarMax Planck Institute for the Science of Light, Erlangen, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We introduce Cryogenic Optical Localization in 3D (COLD), a method to localize multiple fluorescent sites within a single small protein with Angstrom resolution. We demonstrate COLD by determining the conformational state of the cytosolic Per-ARNT-Sim domain from the histidine kinase CitA of Geobacillus thermodenitrificans and resolving the four biotin sites of streptavidin. COLD provides quantitative 3D information about small- to medium-sized biomolecules on the Angstrom scale and complements other techniques in structural biology.

Indexed as

Bacterial ProteinsBinding SitesBiotinCrystallography, X-RayFluorescent DyesFreezingGeobacillusHistidine KinaseImage Processing, Computer-AssistedMagnetic Resonance SpectroscopyMicroscopy, FluorescenceOptics and PhotonicsProtein ConformationProtein DomainsSingle Molecule ImagingStochastic ProcessesBacterial ProteinsBiotinFluorescent DyesHistidine KinaseStreptavidin

Identifiers

PMID28068317

What OpenQuestion holds

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Read underepoch 390

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.