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
Electron Microscope Tomography and Single-particle Reconstruction01:07

Electron Microscope Tomography and Single-particle Reconstruction

2.4K
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...
2.4K
Overview of Electron Microscopy01:25

Overview of Electron Microscopy

9.1K
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.
9.1K
Studying the Cytoskeleton01:17

Studying the Cytoskeleton

6.2K
The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...
6.2K
Super-resolution Fluorescence Microscopy01:37

Super-resolution Fluorescence Microscopy

7.0K
Super-resolution fluorescence microscopy (SRFM) provides a better resolution than conventional fluorescence microscopy by reducing the point spread function (PSF). PSF is the light intensity distribution from a point that causes it to appear blurred. Due to PSF, each fluorescing point appears bigger than its actual size, and it is the PSF interference of nearby fluorophores that causes the blurred image. Various approaches to achieving higher resolution through SRFM have recently been...
7.0K
Crystal Field Theory - Tetrahedral and Square Planar Complexes02:46

Crystal Field Theory - Tetrahedral and Square Planar Complexes

42.5K
Tetrahedral Complexes
Crystal field theory (CFT) is applicable to molecules in geometries other than octahedral. In octahedral complexes, the lobes of the dx2−y2 and dz2 orbitals point directly at the ligands. For tetrahedral complexes, the d orbitals remain in place, but with only four ligands located between the axes. None of the orbitals points directly at the tetrahedral ligands. However, the dx2−y2 and dz2 orbitals (along the Cartesian axes) overlap with the ligands less than the dxy,...
42.5K

You might also read

Related Articles

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

Sort by
Same author

Calicivirus assembly and stability are mediated by the N-terminal domain of the capsid protein with the involvement of the viral genome.

PLoS pathogens·2025
Same author

Nucleic Acid Packaging in Viruses.

Sub-cellular biochemistry·2024
Same author

Observation of Bacteriophage Ultrastructure by Cryo-Electron Microscopy.

Methods in molecular biology (Clifton, N.J.)·2023
Same author

Monitoring reversion of hepatitis C virus-induced cellular alterations by direct-acting antivirals using cryo soft X-ray tomography and infrared microscopy.

Acta crystallographica. Section D, Structural biology·2021
Same author

Assisted assembly of bacteriophage T7 core components for genome translocation across the bacterial envelope.

Proceedings of the National Academy of Sciences of the United States of America·2021
Same author

Using a partial atomic model from medium-resolution cryo-EM to solve a large crystal structure.

Acta crystallographica. Section D, Structural biology·2021

Related Experiment Video

Updated: Jun 30, 2025

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

9.4K

Characterization of Complexes and Supramolecular Structures by Electron Microscopy.

José L Carrascosa1

  • 1Department of Structure of Macromolecules, Centro Nacional de Biotecnología (CNB, CSIC), Madrid, Spain. jlcarras@cnb.csic.es.

Advances in Experimental Medicine and Biology
|March 20, 2024
PubMed
Summary
This summary is machine-generated.

Advancements in cryo-electron microscopy (cryo-TEM) provide near-atomic resolution for macromolecular complexes. This powerful technique offers new insights into drug discovery and cellular biology by revealing dynamic structural changes.

Keywords:
Cryo-electron microscopy (cryo-TEM)Cryo-electron tomography (CET)Direct electron detectors (DED)Electron microscopy (EM)

More Related Videos

Visualizing Proteins and Macromolecular Complexes by Negative Stain EM: from Grid Preparation to Image Acquisition
08:01

Visualizing Proteins and Macromolecular Complexes by Negative Stain EM: from Grid Preparation to Image Acquisition

Published on: December 22, 2011

58.8K
Visualizing Single Molecular Complexes In Vivo Using Advanced Fluorescence Microscopy
11:26

Visualizing Single Molecular Complexes In Vivo Using Advanced Fluorescence Microscopy

Published on: September 8, 2009

9.3K

Related Experiment Videos

Last Updated: Jun 30, 2025

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

9.4K
Visualizing Proteins and Macromolecular Complexes by Negative Stain EM: from Grid Preparation to Image Acquisition
08:01

Visualizing Proteins and Macromolecular Complexes by Negative Stain EM: from Grid Preparation to Image Acquisition

Published on: December 22, 2011

58.8K
Visualizing Single Molecular Complexes In Vivo Using Advanced Fluorescence Microscopy
11:26

Visualizing Single Molecular Complexes In Vivo Using Advanced Fluorescence Microscopy

Published on: September 8, 2009

9.3K

Area of Science:

  • Structural Biology
  • Biophysics
  • Molecular Imaging

Background:

  • Cryo-electron microscopy (cryo-TEM) is a key technique in structural biology.
  • Recent technological improvements have enhanced its capabilities.
  • High resolution allows for the study of macromolecular complexes under physiological conditions.

Purpose of the Study:

  • To highlight recent advancements in cryo-electron microscopy.
  • To discuss the impact of these advancements on structural biology and drug discovery.
  • To explore the potential of cryo-TEM in understanding cellular processes.

Main Methods:

  • Near-atomic resolution imaging of macromolecular complexes.
  • Utilizing enhanced detectors and phase plates for improved signal quality.
  • Application of refined classification methods for conformational state analysis.
  • Employing tomographic procedures for in-situ structural studies.

Main Results:

  • Structures of macromolecular complexes determined at near-atomic resolution.
  • Detection of ligands and substrates under physiological conditions.
  • Reconstruction of smaller macromolecular complexes (below 100 kDa).
  • Identification of diverse conformational states within biological systems.
  • Visualization of subcellular localization and interactions of macromolecular systems.

Conclusions:

  • Cryo-TEM is a pivotal tool in structural biology, enabling near-atomic resolution studies.
  • Technological enhancements are expanding its applications in pharmacology and cell biology.
  • Cryo-TEM provides deep insights into the functional dynamics and cellular context of macromolecular systems.