Evidence map›Paper›PMID 25664622›Full record

ArticleNature nanotechnology2015

Imaging and three-dimensional reconstruction of chemical groups inside a protein complex using atomic force microscopy.

Duckhoe Kim, Ozgur Sahin

Open access · greenAbstract read
In one paragraph

Article in Nature nanotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
3.5field-weighted citation impact, top 7% of its field
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

13 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Article
  3. Resolving Molecular Heterogeneity with Single-Molecule Centrifugation.Journal of the American Chemical Society · 2023
    Article
  4. Article
  5. Biological physics by high-speed atomic force microscopy.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2020
    Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Duckhoe KimDepartments of Biological Sciences and Physics, Columbia University, New York, New York 10027, USA.
Ozgur SahinDepartments of Biological Sciences and Physics, Columbia University, New York, New York 10027, USA.ORCID 0000000327662816
Columbia University · US

Funding

Novel sub-cellular chemical and mechanical nanoimagingDP2EB018657 · NIBIB · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI SAHIN, OZGUR · 2013 to 2013
$2.4M
NCCDPHP CDC HHS 1DP2-EB018657NIBIB NIH HHS DP2 EB018657
6 · The paper itself

Abstract

Scanning probe microscopes can be used to image and chemically characterize surfaces down to the atomic scale. However, the localized tip-sample interactions in scanning probe microscopes limit high-resolution images to the topmost atomic layer of surfaces, and characterizing the inner structures of materials and biomolecules is a challenge for such instruments. Here, we show that an atomic force microscope can be used to image and three-dimensionally reconstruct chemical groups inside a protein complex. We use short single-stranded DNAs as imaging labels that are linked to target regions inside a protein complex, and T-shaped atomic force microscope cantilevers functionalized with complementary probe DNAs allow the labels to be located with sequence specificity and subnanometre resolution. After measuring pairwise distances between labels, we reconstruct the three-dimensional structure formed by the target chemical groups within the protein complex using simple geometric calculations. Experiments with the biotin-streptavidin complex show that the predicted three-dimensional loci of the carboxylic acid groups of biotins are within 2 Å of their respective loci in the corresponding crystal structure, suggesting that scanning probe microscopes could complement existing structural biological techniques in solving structures that are difficult to study due to their size and complexity.

Indexed as

Bacterial ProteinsBiotinDNAImaging, Three-DimensionalMicroscopy, Atomic ForceSequence Analysis, DNABacterial ProteinsBiotinbiotin-streptavidin complexDNA

Identifiers

PMID25664622
PMCPMC4429059
OpenAlexW2001128572

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.