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...

You might also read

Related Articles

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

Sort by

Same author

Hierarchical Functionalisation of UiO-66(Zr)-NH<sub>2</sub> with Cysteine, PEG, and SARS-CoV-2 Spike RBD to Facilitate ACE2 Receptor Targeting in Model Cells.

Nanomaterials (Basel, Switzerland)·2026

Same author

Cryo-EM reveals multiple mechanisms of ribosome inhibition by doxycycline.

Nature communications·2026

Same author

MICOS and MIMAS, multifunctional assemblies linking mitochondrial biogenesis, architecture, and function.

Protein science : a publication of the Protein Society·2026

Same author

Structural insights into the Thermus thermophilus type IV pilus machinery assembling two distinct pili.

Communications biology·2026

Same author

Mitochondria contact lipid droplets through the mitochondrial import complex binding to lipid metabolism enzyme Ayr1.

Nature cell biology·2026

Same author

Monitoring Nanoparticle Interaction with Murine Breast Cancer Cells Using Multimodal Fluorescence Lifetime Microscopy.

International journal of molecular sciences·2026

Same journal

Large-scale discovery and annotation of substructure patterns in mass spectrometry profiles.

Nature communications·2026

Same journal

Salmonella SopB suppresses post-transcriptionally regulated cytokine release to reduce early tissue inflammation and delay disease progression.

Nature communications·2026

Same journal

A human-specific microRNA controls the timing of excitatory synaptogenesis.

Nature communications·2026

Same journal

An HMA-like integrated domain in the wheat tandem kinase WTK4 recognises an RNase-like pathogen effector.

Nature communications·2026

Same journal

Learning regularities in noise engages both neural predictive activity and representational changes.

Nature communications·2026

Same journal

The H3K4 methyltransferase KMT2D is an essential cofactor for GATA1 at erythroid gene enhancers.

Nature communications·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Apr 28, 2026

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

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

Published on: March 5, 2017

Visualizing active membrane protein complexes by electron cryotomography.

Vicki A M Gold¹, Raffaele Ieva², Andreas Walter¹

¹Department of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue-Straße 3, 60438 Frankfurt am Main, Germany.

Nature Communications

|June 20, 2014

Summary

This summary is machine-generated.

Researchers developed a new STAMP technique to visualize active membrane protein complexes in situ using electron cryotomography. This method reveals the 3D organization of mitochondrial protein import sites near crista membranes.

More Related Videos

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Published on: September 14, 2014

Visualization of Organelles In Situ by Cryo-STEM Tomography

Visualization of Organelles In Situ by Cryo-STEM Tomography

Published on: June 23, 2023

Related Experiment Videos

Last Updated: Apr 28, 2026

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

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

Published on: March 5, 2017

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Published on: September 14, 2014

Visualization of Organelles In Situ by Cryo-STEM Tomography

Visualization of Organelles In Situ by Cryo-STEM Tomography

Published on: June 23, 2023

Area of Science:

Cell Biology
Structural Biology
Biophysics

Background:

Understanding membrane protein complexes in their native environment is crucial but challenging.
Visualizing protein machines in their active state requires advanced imaging techniques.

Purpose of the Study:

To develop a novel technique for in situ localization of active membrane protein complexes.
To visualize the three-dimensional organization of mitochondrial protein import sites.

Main Methods:

Developed the Specifically TArgeted Membrane nanoParticle (STAMP) technique.
Utilized electron cryotomography (cryo-ET) with advanced electron detector technology.
Site-specific labeling of membrane proteins using quantum dots.

Main Results:

Visualized the 3D distribution and organization of mitochondrial protein import sites.
Demonstrated that import sites cluster near crista membranes.
Revealed novel details of the mitochondrial protein import machinery in action.

Conclusions:

The STAMP technique enables site-specific labeling of membrane proteins for cryo-ET.
Provides unprecedented insights into the structural organization of active membrane protein machines.
Offers a versatile tool for future studies of membrane protein complexes.