Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Cryo-electron Microscopy

Cryo-electron Microscopy

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...

Electron Microscope Tomography and Single-particle Reconstruction

Electron Microscope Tomography and Single-particle Reconstruction

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...

Atomic Force Microscopy

Atomic Force Microscopy

Atomic force microscopy (AFM) is a type of scanning probe microscopy that can analyze topographic details of various specimens like ceramics, glass, polymers, and biological samples. AFM offers over 1000 times more resolution than the optical imaging system. Images generated from AFM are three-dimensional surface profiles, offering an advantage over the flat, two-dimensional images from other imaging techniques.
The AFM Probe
The probe is regarded as the heart of any AFM setup and comprises the...

You might also read

Related Articles

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

Sort by

Same author

Mechanisms of VEGFR2 activation by VEGF, neuropilin, and heparin.

Science advances·2026

Same author

Structural insights into the activation of the chicken ROS1 receptor by the NEL/NICOL ligand complex.

Nature communications·2026

Same author

Publisher Correction: PtdIns(3,5)P<sub>2</sub> is an endogenous ligand of STING in innate immune signalling.

Nature·2026

Same author

Regulation of STING activation by phosphoinositide and cholesterol.

Nature·2026

Same author

PtdIns(3,5)P<sub>2</sub> is an endogenous ligand of STING in innate immune signalling.

Nature·2026

Same author

Structural basis for ACT1 oligomerization induced by IL-17 receptor hetero-tetramer.

bioRxiv : the preprint server for biology·2026

Search research articles

Related Experiment Video

Updated: Nov 20, 2025

A Robust Single-Particle Cryo-Electron Microscopy cryo-EM Processing Workflow with cryoSPARC, RELION, and Scipion

A Robust Single-Particle Cryo-Electron Microscopy cryo-EM Processing Workflow with cryoSPARC, RELION, and Scipion

Published on: January 31, 2022

Seeing Atoms by Single-Particle Cryo-EM.

Xiao-Chen Bai¹

¹Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX, USA; Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX, USA.

Trends in Biochemical Sciences

|January 25, 2021

Summary

Recent advances in single-particle cryo-electron microscopy (cryo-EM) now allow for atomic-resolution structure determination. This breakthrough enables detailed structural analysis of diverse protein complexes.

Keywords:

atomic resolution single-particle cryo-EM structural biology

More Related Videos

Cryo-EM and Single-Particle Analysis with Scipion

Cryo-EM and Single-Particle Analysis with Scipion

Published on: May 29, 2021

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Published on: May 29, 2021

Related Experiment Videos

Last Updated: Nov 20, 2025

A Robust Single-Particle Cryo-Electron Microscopy cryo-EM Processing Workflow with cryoSPARC, RELION, and Scipion

A Robust Single-Particle Cryo-Electron Microscopy cryo-EM Processing Workflow with cryoSPARC, RELION, and Scipion

Published on: January 31, 2022

Cryo-EM and Single-Particle Analysis with Scipion

Cryo-EM and Single-Particle Analysis with Scipion

Published on: May 29, 2021

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Published on: May 29, 2021

Area of Science:

Structural biology
Biochemistry
Microscopy

Background:

Determining the atomic structure of protein complexes is crucial for understanding biological function.
Traditional methods for high-resolution structure determination are often challenging for large or complex proteins.

Purpose of the Study:

To demonstrate the capability of single-particle cryo-electron microscopy (cryo-EM) for atomic-resolution structure determination.
To highlight the potential of cryo-EM for analyzing a wide range of protein complexes.

Main Methods:

Utilized recent technological advancements in single-particle cryo-electron microscopy (cryo-EM).
Applied cryo-EM techniques to achieve atomic-resolution structural analysis.

Main Results:

Successfully achieved atomic-resolution structure determination using single-particle cryo-EM.
Established cryo-EM as a viable method for high-resolution structural studies.

Conclusions:

Single-particle cryo-EM, with recent technological progress, can now provide atomic-resolution structural information.
This technique expands the possibilities for researchers studying the structure of various protein complexes.