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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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Antibody Structure01:10

Antibody Structure

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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.
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Electron Microscope Tomography and Single-particle Reconstruction01:07

Electron Microscope Tomography and Single-particle Reconstruction

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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: Oct 6, 2025

Single Particle Cryo-Electron Microscopy: From Sample to Structure
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Single Particle Cryo-Electron Microscopy: From Sample to Structure

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From structure to sequence: Antibody discovery using cryoEM.

Aleksandar Antanasijevic1,2, Charles A Bowman1,2, Robert N Kirchdoerfer3

  • 1Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

Science Advances
|January 19, 2022
PubMed
Summary
This summary is machine-generated.

Researchers developed a novel method to identify specific monoclonal antibodies from polyclonal sera using structural and bioinformatic analysis. This breakthrough aids in understanding immune responses and designing better vaccines.

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Area of Science:

  • Structural Biology
  • Bioinformatics
  • Immunology

Background:

  • Monoclonal antibody isolation and characterization are crucial for analyzing immune responses to vaccines and infections.
  • Current methods can be rate-limiting in the study of adaptive immunity.

Purpose of the Study:

  • To present a hybrid structural and bioinformatic approach for direct identification of monoclonal antibodies from polyclonal sera.
  • To enable the discovery of antibody sequences and their functional properties.

Main Methods:

  • Utilized cryo-electron microscopy (cryoEM) density maps of polyclonal antibodies bound to an antigen.
  • Employed a hybrid structural and bioinformatic strategy to assign antibody chains and identify complementarity-determining regions.
  • Integrated next-generation sequencing of immune repertoires.

Main Results:

  • Successfully assigned heavy and light chains and identified complementarity-determining regions directly from cryoEM data.
  • Identified specific clonal family members when combined with next-generation sequencing.
  • Synthesized monoclonal antibodies that functionally matched the original polyclonal antibodies.

Conclusions:

  • This structure-based approach enables the identification of monoclonal antibodies from polyclonal sera.
  • Opens new avenues for analyzing immune responses and iterative vaccine design.
  • Facilitates a deeper understanding of antibody-antigen interactions.