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

Transmission Electron Microscopy01:15

Transmission Electron Microscopy

7.8K
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...
7.8K
Cryo-electron Microscopy01:28

Cryo-electron Microscopy

4.6K
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...
4.6K
Overview of Electron Microscopy01:25

Overview of Electron Microscopy

16.5K
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.
16.5K
Electron Microscope Tomography and Single-particle Reconstruction01:07

Electron Microscope Tomography and Single-particle Reconstruction

3.0K
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
Electron tomography can be performed either in TEM or STEM (scanning transmission...
3.0K
Scanning Electron Microscopy01:07

Scanning Electron Microscopy

5.9K
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...
5.9K
Preparation of Samples for Electron Microscopy01:20

Preparation of Samples for Electron Microscopy

7.7K
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...
7.7K

You might also read

Related Articles

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

Sort by
Same author

Chart builder: an interactive tool for user driven data visualization in the electron microscopy data bank.

Frontiers in bioinformatics·2026
Same author

Candesartan cilexetil disrupts methicillin-resistant Staphylococcus aureus membrane and potentiates gentamicin and polymyxin B activity.

Nature communications·2026
Same author

Primary cortical neurons precipitate and extrude large mitochondria-associated calcium-phosphate sheets with a bone-precursor-like ultrastructure.

Molecular brain·2026
Same author

The relationship between the Ewald sphere and exit wave explored using focal series electron micrographs.

IUCrJ·2025
Same author

The Inaugural Flatiron Institute Cryo-EM Conformational Heterogeneity Challenge.

bioRxiv : the preprint server for biology·2025
Same author

Aviadenovirus structure: A highly thermostable capsid in the absence of stabilizing proteins.

PLoS pathogens·2025

Related Experiment Video

Updated: Mar 25, 2026

Single Particle Electron Microscopy Reconstruction of the Exosome Complex Using the Random Conical Tilt Method
12:10

Single Particle Electron Microscopy Reconstruction of the Exosome Complex Using the Random Conical Tilt Method

Published on: March 28, 2011

24.0K

The Electron Microscopy eXchange (EMX) initiative.

Roberto Marabini1, Steven J Ludtke2, Stephen C Murray3

  • 1Escuela Politecnica Superior, Universidad Autonoma de Madrid, Campus Universidad Autonoma, 28049 Cantoblanco, Madrid, Spain.

Journal of Structural Biology
|February 14, 2016
PubMed
Summary

Standardizing data exchange in cryo-electron microscopy (cryo-EM) is crucial for advancing structural biology. The Electron Microscopy eXchange (EMX) initiative provides a common format for sharing image processing information, enhancing collaboration and data accessibility.

Keywords:
ConventionsData sharingElectron microscopyStandardization

More Related Videos

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

14.1K
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

9.9K

Related Experiment Videos

Last Updated: Mar 25, 2026

Single Particle Electron Microscopy Reconstruction of the Exosome Complex Using the Random Conical Tilt Method
12:10

Single Particle Electron Microscopy Reconstruction of the Exosome Complex Using the Random Conical Tilt Method

Published on: March 28, 2011

24.0K
Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

14.1K
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

9.9K

Area of Science:

  • Structural Biology
  • Biophysics
  • Computational Biology

Background:

  • Three-dimensional electron microscopy (3DEM) enables near-native structural analysis of large biomolecules.
  • Progress in cryo-electron microscopy (cryo-EM) is closely linked to advancements in image processing software.
  • Data and methods sharing in cryo-EM is hindered by a lack of standardized formats across different software packages.

Purpose of the Study:

  • To introduce the Electron Microscopy eXchange (EMX) initiative and its version 1.0 conventions.
  • To establish a standard for exchanging information in single-particle analysis within cryo-EM.
  • To facilitate seamless collaboration and data sharing among different cryo-EM software platforms.

Main Methods:

  • Development of the Electron Microscopy eXchange (EMX) version 1.0 standard.
  • Specification of metadata for micrograph and particle images, including CTF parameters and particle orientations.
  • Implementation of EMX v1.0 in major cryo-EM image processing packages (Bsoft, EMAN, Xmipp, Scipion).

Main Results:

  • EMX v1.0 provides a standardized convention for cryo-EM data interchange.
  • The standard covers essential metadata for single-particle analysis, including image parameters and particle orientations.
  • EMX v1.0 has been adopted by key software packages and validation challenges.

Conclusions:

  • Standardization through EMX is essential for the future progress of cryo-EM data and methods sharing.
  • EMX facilitates interoperability between different software packages, promoting collaboration.
  • The EMX initiative supports data archiving and validation efforts in structural biology.