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Related Concept Videos

Cryo-electron Microscopy01:28

Cryo-electron Microscopy

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Conventional electron microscopy (EM) involves dehydration, fixation, and staining of biological samples, which distorts the native state of biological molecules and results in several artifacts. Also, the high-energy electron beam damages the sample and makes it difficult to obtain high-resolution images. These issues can be addressed using cryo-EM, which uses frozen samples and gentler electron beams. The technique was developed by Jacques Dubochet, Joachim Frank, and Richard Henderson, for...
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Electron Microscope Tomography and Single-particle Reconstruction01:07

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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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Related Experiment Video

Updated: Jun 30, 2025

A Pipeline to Investigate the Structures and Signaling Pathways of Sphingosine 1-Phosphate Receptors
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Cryo-EM advances in GPCR structure determination.

Wataru Shihoya1, Aika Iwama1, Fumiya K Sano1

  • 1Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-Ku, Tokyo 113-0033, Japan.

Journal of Biochemistry
|March 18, 2024
PubMed
Summary

Cryo-electron microscopy (cryo-EM) advances structural understanding of G-protein-coupled receptors (GPCRs). This review details how cryo-EM, with tools like nanobodies, reveals GPCR activation mechanisms for drug discovery.

Keywords:
G-protein-coupled receptorcryo-EMstructural biology

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Area of Science:

  • Biochemistry and Structural Biology
  • Molecular and Cellular Biology

Background:

  • G-protein-coupled receptors (GPCRs) are crucial for cellular communication and drug targets.
  • High-resolution structural data for GPCRs has been historically challenging to obtain.
  • GPCRs are classified into six distinct families (A-F).

Purpose of the Study:

  • To review the impact of cryogenic electron microscopy (cryo-EM) on determining GPCR-G-protein complex structures.
  • To highlight technologies that aid in GPCR structural determination.
  • To discuss structural changes during GPCR activation across different classes.

Main Methods:

  • Cryogenic electron microscopy (cryo-EM) for high-resolution structural analysis.
  • Use of stabilizing agents like nanobodies and mini-G-proteins.
  • Comparative analysis of structural data across different GPCR classes.

Main Results:

  • Cryo-EM has overcome previous limitations in acquiring high-resolution GPCR structures.
  • Nanobodies and mini-G-proteins effectively stabilize GPCR-G-protein complexes for imaging.
  • Diverse structural alterations upon activation have been elucidated for various GPCR classes.

Conclusions:

  • Cryo-EM provides a robust foundation for understanding GPCR structure and function.
  • This structural insight is critical for advancing drug discovery and therapeutic targeting of GPCRs.
  • Future research will likely leverage cryo-EM for novel GPCR-based therapeutics.