Structure Characterization of Bacterial Microcompartment Shells via X-ray Scattering and Coordinate Modeling: Evidence for Adventitious Capture of Cytoplasmic Proteins.
Article in ACS applied bio materials, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
0numbers the graph read from it
0cells of the map it votes in
1citing 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.
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
14 authors.
Xiaobing ZuoX-ray Science Division, Argonne National Laboratory, Lemont, Illinois 60439, United States.
Alexander JussupowDepartment of Biochemistry & Molecular Biology, Michigan State University, East Lansing, Michigan 48824, United States.
Nina S PonomarenkoChemical Sciences and Engineering Division, Argonne National Laboratory, Lemont, Illinois 60439, United States.ORCID 0000-0001-7256-3126
Thomas D GrantDepartment of Structural Biology, Jacobs School of Medicine and Biomedical Sciences, SUNY University at Buffalo, Buffalo, New York 14203, United States.ORCID 0000-0002-8583-3700
Nicholas M TefftDepartment of Biochemistry & Molecular Biology, Michigan State University, East Lansing, Michigan 48824, United States.
Neetu Singh YadavDepartment of Biochemistry & Molecular Biology, Michigan State University, East Lansing, Michigan 48824, United States.
Kyleigh L RangeMSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824, United States.
Corie Y RalstonMolecular Foundry Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, United States.ORCID 0000-0002-7899-0951
Michaela A TerAvestDepartment of Biochemistry & Molecular Biology, Michigan State University, East Lansing, Michigan 48824, United States.ORCID 0000-0002-5435-3587
Markus SutterMSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824, United States.
Cheryl A KerfeldMSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824, United States.ORCID 0000-0002-9977-8482
Josh V VermaasDepartment of Biochemistry & Molecular Biology, Michigan State University, East Lansing, Michigan 48824, United States.ORCID 0000-0003-3139-6469
Michael FeigDepartment of Biochemistry & Molecular Biology, Michigan State University, East Lansing, Michigan 48824, United States.
David M TiedeChemical Sciences and Engineering Division, Argonne National Laboratory, Lemont, Illinois 60439, United States.ORCID 0000-0002-2784-4954
Funding
High-resolution molecular recognition of ligands using solution X-ray scatteringR01GM133998 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI GRANT, THOMAS D. · 2019 to 2022
$1.3M
NIGMS NIH HHS R01 GM133998
6 · The paper itself
Abstract
Bacterial microcompartments (BMCs) are self-assembling protein shell structures that are widely investigated across a broad range of biological and abiotic chemistry applications. A central challenge in BMC research is the targeted capture of enzymes during shell assembly. While crystallography and cryo-EM techniques have been successful in determining BMC shell structures, there has been only limited success in visualizing the location of BMC-captured enzyme cargo. Here, we demonstrate the opportunity to use small-angle X-ray scattering (SAXS) and pair distance distribution function (PDDF) measurements combined with quantitative comparison to coordinate structure models as an approach to characterize BMC shell structures in solution conditions directly relevant to biochemical function. Using this approach, we analyzed BMC shells from
Indexed as
Bacterial ProteinsBiocompatible MaterialsEscherichia coliMaterials TestingModels, MolecularParticle SizeScattering, Small AngleX-Ray DiffractionBacterial ProteinsBiocompatible Materialsbacterial microcompartmentsDAMMINDENSS (DENsity from Solution Scattering)molecular dynamics (MD)pair distance distribution function (PDDF)SAXS ab initio structuresmall-angle X-ray scattering (SAXS)
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.
Structure Characterization of Bacterial Microcompartment Shells via X-ray Scattering and Coordinate Modeling: Evidence for Adventitious Capture of Cytoplasmic Proteins. · full record | OpenQuestion