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Transmission electron microscopy (TEM) can be used to determine the 3D structure of biological samples with the help of techniques such as electron microscope tomography and single-particle reconstruction. While single-particle reconstruction can examine macromolecules and macromolecular complexes in vitro conditions only, tomography permits the study of cell components or small cells in vivo.
Electron Tomography
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High Precision FRET at Single-molecule Level for Biomolecule Structure Determination

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In situ structure determination at nanometer resolution using TYGRESS.

Kangkang Song^1,2, Zhiguo Shang¹, Xiaofeng Fu^1,3

¹Departments of Cell Biology and Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, USA.

|November 27, 2019

Summary

This summary is machine-generated.

We developed TYGRESS, a hybrid cryo-electron tomography and single-particle cryo-electron microscopy method. This technique achieves near-nanometer resolution for cellular structures within crowded environments.

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Area of Science:

Structural biology
Cell biology
Microscopy techniques

Background:

Cryo-electron tomography (cryo-ET) resolution is limited in crowded cellular environments due to signal loss and misalignment.
Single-particle cryo-electron microscopy (SP-cryo-EM) achieves high resolution for isolated complexes but is unsuitable for in situ structural determination.
There is a need for methods to resolve macromolecular structures within their native cellular context at high resolution.

Purpose of the Study:

To develop a hybrid method combining cryo-ET and SP-cryo-EM for high-resolution structural determination of cellular complexes in situ.
To overcome the limitations of traditional cryo-ET in crowded cellular environments.
To enable visualization of structural details not achievable with cryo-ET alone.

Main Methods:

Introduced TYGRESS (tomography-guided 3D reconstruction of subcellular structures), a hybrid approach integrating cryo-ET and SP-cryo-EM.
Leveraged the high signal-to-noise ratio and contrast from SP-cryo-EM with the 3D alignment capabilities of subtomogram averaging.
Applied TYGRESS to determine the structure of the intact ciliary axoneme.

Main Results:

Achieved close-to-nanometer resolution for macromolecular complexes within crowded cellular environments.
Determined the structure of the intact ciliary axoneme with a resolution of up to 12 Å.
Revealed previously unresolvable structural details of cellular components in situ.

Conclusions:

TYGRESS effectively combines the strengths of cryo-ET and SP-cryo-EM for high-resolution structural biology in cellular contexts.
The method is broadly applicable to various cellular complexes amenable to subtomogram averaging.
TYGRESS significantly advances the capability to study molecular structures within their native cellular environment.