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Related Experiment Video

Universal Molecular Retention with 11-Fold Expansion Microscopy
10:31

Universal Molecular Retention with 11-Fold Expansion Microscopy

Published on: October 6, 2023

Thousandfold Expansion Microscopy.

Helena Hu, Donatus Krah, Antonios Ntolkeras

    Biorxiv : the Preprint Server for Biology
    |June 12, 2026

    View abstract on PubMed

    Summary
    This summary is machine-generated.

    Thousandfold expansion microscopy (1000ExM) images individual protein residues by anchoring and expanding them. This novel technique achieves sub-nanometer precision, enabling detailed protein visualization.

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    Area of Science:

    • Biochemistry
    • Microscopy
    • Materials Science

    Background:

    • Proteins are essential biological macromolecules composed of amino acid residues.
    • Current imaging techniques face limitations in resolving individual amino acid residues within proteins.

    Purpose of the Study:

    • To develop a novel microscopy technique for visualizing individual protein residues.
    • To achieve sub-nanometer precision in imaging protein structures.

    Main Methods:

    • Anchoring protein side chains to a swellable polymer.
    • Cleaving backbone amide bonds to separate residues.
    • Utilizing a four-network interpenetrating hydrogel architecture for successive expansion (1000ExM).

    Main Results:

    • Achieved successive expansion up to >1000-fold (one billion-fold in volume).
    • Maintained protein and peptide structures across expansion factors.
    • Demonstrated resolution of adjacent amino acid residues, achieving sub-nanometer precision.

    Conclusions:

    • 1000ExM enables visualization of individual protein residues with unprecedented precision.
    • This technique offers potential for wide application in protein visualization and identification.
    • 1000ExM may be applicable in intact cells and tissues.