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Updated: Jun 13, 2026

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

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Published on: October 6, 2023

Thousandfold Expansion Microscopy.

Helena Hu1, Donatus Krah2, Antonios Ntolkeras2

  • 1Department of Biological Engineering, MIT, Cambridge, MA 02139.

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