Evidence map›Paper›PMID 28973937›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Detection of isolated protein-bound metal ions by single-particle cryo-STEM.

Nadav Elad, Giuliano Bellapadrona, Lothar Houben, Irit Sagi, Michael Elbaum

Open access · bronzeAbstract readEvaluation Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.7field-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

15 citing papers in PubMed, 59 citations in OpenAlex.

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  8. Charting the molecular landscape of the cell.Structure (London, England : 1993) · 2023
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  14. Three-dimensional deconvolution processing for STEM cryotomography.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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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 at 1 institution in 1 country.

Nadav EladElectron Microscopy Unit, Department of Chemical Research Support, Weizmann Institute of Science, Rehovot 7610001, Israel.
Giuliano BellapadronaDepartment of Materials and Interfaces, Weizmann Institute of Science, Rehovot 7610001, Israel.
Lothar HoubenElectron Microscopy Unit, Department of Chemical Research Support, Weizmann Institute of Science, Rehovot 7610001, Israel.
Irit SagiDepartment of Biological Regulation, Weizmann Institute of Science, Rehovot 7610001, Israel.
Michael ElbaumDepartment of Materials and Interfaces, Weizmann Institute of Science, Rehovot 7610001, Israel; michael.elbaum@weizmann.ac.il.
Weizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Metal ions play essential roles in many aspects of biological chemistry. Detecting their presence and location in proteins and cells is important for understanding biological function. Conventional structural methods such as X-ray crystallography and cryo-transmission electron microscopy can identify metal atoms on protein only if the protein structure is solved to atomic resolution. We demonstrate here the detection of isolated atoms of Zn and Fe on ferritin, using cryogenic annular dark-field scanning transmission electron microscopy (cryo-STEM) coupled with single-particle 3D reconstructions. Zn atoms are found in a pattern that matches precisely their location at the ferroxidase sites determined earlier by X-ray crystallography. By contrast, the Fe distribution is smeared along an arc corresponding to the proposed path from the ferroxidase sites to the mineral nucleation sites along the twofold axes. In this case the single-particle reconstruction is interpreted as a probability distribution function based on the average of individual locations. These results establish conditions for detection of isolated metal atoms in the broader context of electron cryo-microscopy and tomography.

Indexed as

Cryoelectron MicroscopyFerritinsIronMicroscopy, Electron, Scanning TransmissionZincFerritinsIronZinccryo-microscopymetalloproteinprotein structurescanning transmission electron microscopysingle-particle analysis

Identifiers

PMID28973937
PMCPMC5651765
OpenAlexW2760824416

What OpenQuestion holds

Textmetadata
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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.