Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Cryo-electron Microscopy01:28

Cryo-electron Microscopy

3.3K
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...
3.3K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Cryo-electron microscopy structures of human cone visual pigments.

Science (New York, N.Y.)·2026
Same author

Inhibitory effects and structural analysis of drug candidate PF-07817883 against coronaviral main proteases (M<sup>pro</sup>) and SARS-CoV-2 M<sup>pro</sup> mutants.

Journal of structural biology: X·2026
Same author

Discovery of a potential CERS2 inhibitor: hit compound identification via structure-based virtual screening and molecular dynamics simulations.

Molecular diversity·2026
Same author

The Emerging Mycotoxin 2-Amino-14, 16-Dimethyloctadecan-3-ol (AOD) Alters Transcriptional Regulation and Sphingolipid Metabolism and Undergoes <i>N</i>-Acylation by HepG2 Cells.

Toxins·2025
Same author

Analysis of Epidemiological and Evolutionary Characteristics of Seasonal Influenza Viruses in Shenzhen City from 2018 to 2024.

Viruses·2025
Same author

Structural basis for the inhibition of coronaviral main proteases by PF-00835231.

Acta biochimica et biophysica Sinica·2024

Related Experiment Video

Updated: Jun 16, 2025

High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE
13:28

High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE

Published on: May 16, 2017

50.3K

Structural analysis of the human C5a-C5aR1 complex using cryo-electron microscopy.

Tingting Yang1, Jian Li2, Xinyu Cheng1

  • 1The MOE Basic Research and Innovation Center for the Targeted Therapeutics of Solid Tumors, School of Basic Medical Sciences, Jiangxi Medical College, Nanchang University, Nanchang 330031, China; The Second Affiliated Hospital, Jiangxi Medical College, Nanchang University, Nanchang 330006, China.

Journal of Structural Biology
|August 17, 2024
PubMed
Summary
This summary is machine-generated.

Researchers elucidated the structure of the C5a-C5aR1-Gi complex using cryo-electron microscopy. This reveals key insights into complement system function and potential drug targets for immune response modulation.

Keywords:
C5aR1Complement systemCryo‐electron microscopyG protein‐coupled receptor (GPCR)Structure

More Related Videos

Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction
09:25

Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction

Published on: January 9, 2015

46.1K
Single Particle Cryo-Electron Microscopy: From Sample to Structure
11:52

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Published on: May 29, 2021

8.4K

Related Experiment Videos

Last Updated: Jun 16, 2025

High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE
13:28

High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE

Published on: May 16, 2017

50.3K
Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction
09:25

Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction

Published on: January 9, 2015

46.1K
Single Particle Cryo-Electron Microscopy: From Sample to Structure
11:52

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Published on: May 29, 2021

8.4K

Area of Science:

  • Immunology
  • Structural Biology
  • Biochemistry

Background:

  • The complement system is vital for innate immunity, with the C5a-C5aR1 complex mediating immune cell recruitment and activation.
  • Understanding C5a-C5aR1 activation and signaling is crucial for C5a-mediated disease research.

Purpose of the Study:

  • To determine the high-resolution structure of the C5a-C5aR1-Gi complex.
  • To investigate the C5a binding site and its impact on receptor conformation and signaling.
  • To identify key residues regulating C5a-mediated signaling pathways.

Main Methods:

  • Cryo-electron microscopy (Cryo-EM) was employed to determine the structure of the C5a-C5aR1-Gi complex at 3 Å resolution.

Main Results:

  • The study identified the C5a binding site, involving extracellular polar interactions and a transmembrane amphipathic pocket.
  • C5a binding induces conformational changes in C5aR1, activating G protein signaling.
  • Residue M265 on TM6 was found to be critical for regulating C5a-induced β-arrestin recruitment.

Conclusions:

  • This research provides detailed structural and functional information on the human C5a-C5aR1 complex, essential for complement system function.
  • The findings offer a foundation for developing targeted pharmaceuticals with specific or biased signaling for the C5a receptor.