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

3.6K
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...
3.6K
Antibody Structure01:10

Antibody Structure

61.3K
Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
61.3K

You might also read

Related Articles

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

Sort by
Same author

Structural Dynamics of RNA Polymerase II During Nucleotide Addition Cycle.

bioRxiv : the preprint server for biology·2026
Same author

Structural and functional characterisation of the Crimean-Congo haemorrhagic fever virus RNA dependent RNA polymerase.

Nature communications·2026
Same author

Structural Advances in Respiratory Syncytial Virus: Implications for Vaccine and Antiviral Development.

Microorganisms·2026
Same author

Sub-2 Å cryo-EM structures of transcribing RNA polymerase II reveal critical roles of water molecules in catalysis.

Molecular cell·2026
Same author

SPNS2 exports sphingosine-1-phosphate and imports glucose.

Nature communications·2026
Same author

Live-cell 3D-SIM of Rift Valley fever virus NSs filaments reveals a polygon web architecture.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Cryo-EM sheds light on the mechanism of human telomerase inhibition by BIBR1532.

Nature chemical biology·2026
Same journal

Artificial metalloenzymes in complex biological environments.

Nature chemical biology·2026
Same journal

Allosteric disordering of eIF2B regulates the integrated stress response.

Nature chemical biology·2026
Same journal

A tail of two ligases.

Nature chemical biology·2026
Same journal

Non-canonical cytochrome P450 enzymes expand the diversity of bacterial hemoproteins.

Nature chemical biology·2026
Same journal

Image-guided activation of drugs with electromagnetic radiation.

Nature chemical biology·2026
See all related articles

Related Experiment Video

Updated: Sep 11, 2025

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

12.8K

Covalently constrained 'Di-Gembodies' enable parallel structure solutions by cryo-EM.

Gangshun Yi1,2,3, Dimitrios Mamalis4,5, Mingda Ye6

  • 1Division of Structural Biology, Centre for Human Genetics, University of Oxford, Oxford, UK.

Nature Chemical Biology
|August 15, 2025
PubMed
Summary
This summary is machine-generated.

Di-Gembodies, engineered nanobody dimers, enable high-resolution cryo-electron microscopy (cryo-EM) for small proteins. This flexible platform enhances protein structure determination by improving particle alignment and increasing throughput.

More Related Videos

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps
09:30

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps

Published on: July 19, 2024

1.5K
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

8.8K

Related Experiment Videos

Last Updated: Sep 11, 2025

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

12.8K
Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps
09:30

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps

Published on: July 19, 2024

1.5K
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

8.8K

Area of Science:

  • Structural biology
  • Biochemistry
  • Biophysics

Background:

  • Cryo-electron microscopy (cryo-EM) is vital for structural biology but faces challenges with small proteins (<100 kDa).
  • Existing protein scaffolds for cryo-EM can be inadequate or limited in availability.
  • Improved particle alignment and increased protein size are crucial for high-resolution cryo-EM structure determination.

Purpose of the Study:

  • To develop a novel strategy for enhancing cryo-EM structure determination of small proteins.
  • To introduce modular constructs (Di-Gembodies) for improved protein size and particle alignment.
  • To provide a flexible and scalable platform for expanded protein structure determination.

Main Methods:

  • Exploiting covalent dimerization of nanobodies to create Di-Gembodies.
  • Utilizing a predisposed nanobody-to-nanobody interface for engineered assembly.
  • Employing side-chain-to-side-chain assembly to display proteins in homomeric or heteromeric forms.

Main Results:

  • Demonstrated successful cryo-EM structure determination for multiple soluble and membrane protein targets.
  • Validated the method for proteins as small as 14 kDa.
  • Showcased Di-Gembodies as modular constructs providing sufficient constraint for structure determination.

Conclusions:

  • Di-Gembodies offer a flexible and scalable platform for cryo-EM structure determination.
  • The covalent dimerization strategy effectively overcomes limitations in analyzing small proteins.
  • This approach expands the scope and throughput of cryo-EM studies for challenging targets.