Evidence map›Paper›PMID 26617073›Full record

ArticleNano letters2016

Visualization of Bacterial Microcompartment Facet Assembly Using High-Speed Atomic Force Microscopy.

Markus Sutter, Matthew Faulkner, Clément Aussignargues, Bradley C Paasch, Steve Barrett, Cheryl A Kerfeld, Lu-Ning Liu

Open access · hybridAbstract read
In one paragraph

Article in Nano letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

62 citing papers in PubMed, 117 citations in OpenAlex.

  1. Article
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  5. Chemical reviews · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Interfacing bacterial microcompartment shell proteins with genetically encoded condensates.Protein science : a publication of the Protein Society · 2025
    Article
  11. Article
  12. Article
  13. Review
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  16. Article
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  20. Article

2 more citing papers are in PubMed but not listed here.

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

7 authors at 2 institutions in 1 country.

Markus SutterMSU-DOE Plant Research Laboratory, Michigan State University , East Lansing, Michigan 48824, United States.
Matthew Faulkner
Clément AussignarguesMSU-DOE Plant Research Laboratory, Michigan State University , East Lansing, Michigan 48824, United States.
Bradley C PaaschMSU-DOE Plant Research Laboratory, Michigan State University , East Lansing, Michigan 48824, United States.
Steve Barrett
Cheryl A KerfeldMSU-DOE Plant Research Laboratory, Michigan State University , East Lansing, Michigan 48824, United States.
Lu-Ning Liu
Michigan State University · USLawrence Berkeley National Laboratory · US

Funding

Structure and Function of Bacterial Microcompartment Shells from Human PathogensR01AI114975 · NIAID · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI KERFELD, CHERYL A · 2015 to 2022
$3.0M
Biotechnology and Biological Sciences Research Council BB/M012441/1Biotechnology and Biological Sciences Research Council BB/M024202/1NIAID NIH HHS 1R01AI114975-01NIAID NIH HHS R01 AI114975
6 · The paper itself

Abstract

Bacterial microcompartments (BMCs) are proteinaceous organelles widespread among bacterial phyla. They compartmentalize enzymes within a selectively permeable shell and play important roles in CO2 fixation, pathogenesis, and microbial ecology. Here, we combine X-ray crystallography and high-speed atomic force microscopy to characterize, at molecular resolution, the structure and dynamics of BMC shell facet assembly. Our results show that preformed hexamers assemble into uniformly oriented shell layers, a single hexamer thick. We also observe the dynamic process of shell facet assembly. Shell hexamers can dissociate from and incorporate into assembled sheets, indicating a flexible intermolecular interaction. Furthermore, we demonstrate that the self-assembly and dynamics of shell proteins are governed by specific contacts at the interfaces of shell proteins. Our study provides novel insights into the formation, interactions, and dynamics of BMC shell facets, which are essential for the design and engineering of self-assembled biological nanoreactors and scaffolds based on BMC architectures.

Indexed as

Bacterial ProteinsCrystallography, X-RayMicroscopy, Atomic ForceMyxococcalesPoint MutationProtein ConformationBacterial ProteinsBacterial microcompartmenthigh-speed atomic force microscopyprotein dynamicsprotein interactionself-assembly

Identifiers

PMID26617073
PMCPMC4789755
OpenAlexW2219945828

What OpenQuestion holds

Textmetadata
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.