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Updated: Jun 12, 2026

Multi-color Localization Microscopy of Single Membrane Proteins in Organelles of Live Mammalian Cells

Multi-color Localization Microscopy of Single Membrane Proteins in Organelles of Live Mammalian Cells

Published on: June 30, 2018

Precise mapping of subunits in multiprotein complexes by a versatile electron microscopy label.

Dirk Flemming¹, Karsten Thierbach, Philipp Stelter

¹Biochemie-Zentrum der Universität Heidelberg, Heidelberg, Germany.

Nature Structural & Molecular Biology

|June 1, 2010

Summary

Researchers developed a new tag to precisely map protein subunit positions in large molecular complexes using electron microscopy. This method enhances the visualization and topological analysis of macromolecular assemblies.

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Proteome-wide Quantification of Labeling Homogeneity at the Single Molecule Level

Proteome-wide Quantification of Labeling Homogeneity at the Single Molecule Level

Published on: April 19, 2019

Area of Science:

Structural biology
Molecular biology
Biochemistry

Background:

Understanding multiprotein assembly function requires precise knowledge of subunit positions.
Electron microscopy (EM) has advanced topological analysis of protein complexes, but pinpointing single subunit locations remains challenging.

Purpose of the Study:

To develop a novel method for the exact topological mapping of single subunits within macromolecular complexes.
To create a versatile tag for recruiting EM labels to target proteins.

Main Methods:

Development of a clonable, approximately 80-residue tag for specific protein attachment.
In vitro recruitment of a prominent electron microscopy label to the tagged protein.
Utilizing single-particle electron microscopy with advanced image processing and classification.

Main Results:

The developed tag is easily attached to target proteins.
The tag is visible on single particles and becomes highly distinct after image processing.
The method enables precise visualization of subunit positions within complexes.

Conclusions:

The new tag facilitates accurate topological mapping of subunits in macromolecular complexes.
This technique significantly improves the analysis of protein complex architecture.
The method is broadly applicable for studying the structure and function of protein assemblies.