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

4.2K
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...
4.2K
Overview of Electron Microscopy01:25

Overview of Electron Microscopy

13.6K
The wavelengths of visible light ultimately limit the maximum theoretical resolution of images created by light microscopes. Most light microscopes can only magnify 1000X, and a few can magnify up to 1500X. Electrons, like electromagnetic radiation, can behave like waves, but with wavelengths of 0.005 nm, they produce significantly greater resolution up to 0.05 nm as compared to 500 nm for visible light. An electron microscope (EM) can create a sharp image that is magnified up to 2,000,000X.
13.6K
Scanning Electron Microscopy01:07

Scanning Electron Microscopy

5.4K
A scanning electron microscope (SEM) is used to study the surface features of a sample by using an electron beam that scans the sample surface in a two-dimensional manner. Typically, areas between ~1 centimeter to 5 micrometers in width can be imaged. SEM can be used to image bacteria, viruses, tissues as well as larger samples like insects. Conventional SEM gives a magnification ranging from 20X to 30,000X and spatial resolution of 50 to 100 nanometers.
Fundamental Principles
Accelerated...
5.4K
Transmission Electron Microscopy01:15

Transmission Electron Microscopy

6.9K
In 1931, physicist Ernst Ruska—building on the idea that magnetic fields can direct an electron beam just as lenses can direct a beam of light in an optical microscope—developed the first prototype of the electron microscope. This development led to the development of the field of electron microscopy. In the transmission electron microscope (TEM), electrons are produced by a hot tungsten element and accelerated by a potential difference in an electron gun, which gives them up to 400...
6.9K
Immunogold Electron Microscopy01:20

Immunogold Electron Microscopy

5.4K
Immunoelectron microscopy utilizes immunogold labeling of endogenous proteins with specific antibodies to detect and localize these proteins in cells and tissues. The procedure provides insights into the distribution and quantification of protein under different stimulation conditions offering clues about their functions. Conjugating highly electron-dense gold particles with primary or secondary antibodies allow antigen detection on and within cells, with high resolution and specificity.
5.4K
Preparation of Samples for Electron Microscopy01:20

Preparation of Samples for Electron Microscopy

6.9K
To be visualized by an electron microscope, either transmission or scanning, biological samples need to be fixed (stabilized) so the electron beam does not destroy them and dried thoroughly (desiccated/dehydrated) so the vacuum does not affect them. Fixation needs to be done as quickly as possible because the sample properties will start changing as soon as it is removed from its natural environment. For example, in a tissue sample, the oxygen levels begin decreasing, causing an altered...
6.9K

You might also read

Related Articles

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

Sort by
Same author

Atomic resolution cryo-EM at 200 keV.

IUCrJ·2026
Same author

CCDC32 collaborates with the membrane to assemble the AP-2 clathrin adaptor complex.

Science advances·2026
Same author

Cryo-EM reveals ArnA contamination during purification of a ciliary protein complex.

Acta crystallographica. Section D, Structural biology·2026
Same author

Oligomerization-Dependent Regulation of LrhA Controls Bacterial Flagellar Biosynthesis.

Journal of molecular biology·2026
Same author

Motor protein tails: Hidden order within disorder.

Molecular biology of the cell·2025
Same author

Functional landscape of mechanistic diversity in 27 claudin family members at tight junctions.

Science advances·2025
Same journal

Drugging the proteome via large-scale chemoproteomics.

Trends in biochemical sciences·2026
Same journal

Peptideins: Navigating the gray zone of the proteome.

Trends in biochemical sciences·2026
Same journal

A metabolon channels nicotine biosynthesis.

Trends in biochemical sciences·2026
Same journal

Better call chaperone.

Trends in biochemical sciences·2026
Same journal

Biochemistry at scale: Seeing both the forest and the trees.

Trends in biochemical sciences·2026
Same journal

Voices across Asia and Oceania: Biochemistry across borders.

Trends in biochemical sciences·2026
See all related articles

Related Experiment Video

Updated: Jan 25, 2026

Micropatterning Transmission Electron Microscopy Grids to Direct Cell Positioning within Whole-Cell Cryo-Electron Tomography Workflows
09:53

Micropatterning Transmission Electron Microscopy Grids to Direct Cell Positioning within Whole-Cell Cryo-Electron Tomography Workflows

Published on: September 13, 2021

7.6K

Cryo-Electron Microscopy Methodology: Current Aspects and Future Directions.

Radostin Danev1, Haruaki Yanagisawa1, Masahide Kikkawa1

  • 1Graduate School of Medicine, The University of Tokyo, Tokyo 113-0033, Japan.

Trends in Biochemical Sciences
|May 13, 2019
PubMed
Summary
This summary is machine-generated.

Cryo-electron microscopy (cryo-EM) offers powerful protein structure determination through single particle analysis (SPA) and cryo-electron tomography (cryo-ET). Methodological improvements in cryo-EM will enhance reliability, throughput, and accessibility.

Keywords:
cryo-electron microscopycryo-electron tomography, 3D reconstructionsingle particle analysis

More Related Videos

Author Spotlight: Enhancing Cryo-Electron Microscopy by Automated Data Collection and Analysis Techniques
07:52

Author Spotlight: Enhancing Cryo-Electron Microscopy by Automated Data Collection and Analysis Techniques

Published on: December 1, 2023

1.5K
Cryo-electron Microscopy Specimen Preparation By Means Of a Focused Ion Beam
10:54

Cryo-electron Microscopy Specimen Preparation By Means Of a Focused Ion Beam

Published on: July 26, 2014

27.2K

Related Experiment Videos

Last Updated: Jan 25, 2026

Micropatterning Transmission Electron Microscopy Grids to Direct Cell Positioning within Whole-Cell Cryo-Electron Tomography Workflows
09:53

Micropatterning Transmission Electron Microscopy Grids to Direct Cell Positioning within Whole-Cell Cryo-Electron Tomography Workflows

Published on: September 13, 2021

7.6K
Author Spotlight: Enhancing Cryo-Electron Microscopy by Automated Data Collection and Analysis Techniques
07:52

Author Spotlight: Enhancing Cryo-Electron Microscopy by Automated Data Collection and Analysis Techniques

Published on: December 1, 2023

1.5K
Cryo-electron Microscopy Specimen Preparation By Means Of a Focused Ion Beam
10:54

Cryo-electron Microscopy Specimen Preparation By Means Of a Focused Ion Beam

Published on: July 26, 2014

27.2K

Area of Science:

  • Structural biology
  • Biophysics
  • Biochemistry

Background:

  • Cryo-electron microscopy (cryo-EM) is a key technique for determining molecular structures.
  • Single particle analysis (SPA) and cryo-electron tomography (cryo-ET) are major cryo-EM methods.
  • Cryo-EM enables visualization of proteins and complexes in near-native states.

Purpose of the Study:

  • To review the current state of cryo-electron microscopy.
  • To identify areas for methodological improvement in cryo-EM.
  • To project future developments in cryo-EM technology.

Main Methods:

  • Review of single particle analysis (SPA) and cryo-electron tomography (cryo-ET) principles.
  • Analysis of current challenges in sample preparation, screening, data acquisition, image processing, and structure validation.
  • Discussion of potential advancements to enhance cryo-EM capabilities.

Main Results:

  • Cryo-EM, particularly SPA and cryo-ET, is widely used for high-resolution protein structure determination.
  • Several methodological aspects of cryo-EM require improvement for broader application.
  • Key areas for advancement include sample handling, data collection, and computational analysis.

Conclusions:

  • Cryo-EM is a powerful and increasingly adopted technique for structural biology.
  • Future developments are expected to improve cryo-EM's reliability, efficiency, and ease of use.
  • Advancements will lower barriers to entry, making cryo-EM more accessible to researchers worldwide.