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...

You might also read

Related Articles

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

Sort by

Same author

Large-Scale Structural Dynamics in the Tail Fiber Modulate the Infective Transition of the T7 Bacteriophage.

Small (Weinheim an der Bergstrasse, Germany)·2026

Same author

Considerations for Pre-deployment Planning in Point-of-Care Ultrasound Program Implementation: A HIMSS-SIIM Enterprise Imaging Community Whitepaper in Collaboration with AIUM.

Journal of imaging informatics in medicine·2026

Same author

Physicochemical, structural, and immunological characterization of recombinant Mal d 1.02 allergen in Mexican pediatric patients. A valuable tool for diagnosing.

Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association·2026

Same author

Editorial: Modeling the immune system: from PK/PD to systems immunology.

Frontiers in immunology·2026

Same author

Structures of <i>Vibrio cholerae</i> transcription complexes reveal how ToxR and TcpP recruit the RNA polymerase and activate virulence genes.

Science advances·2026

Same author

Effect of a fructooligosaccharides fraction from <i>Psacalium decompositum</i> on the intestinal bacterial microbiota of rats.

Bioscience of microbiota, food and health·2026

Same journal

Scotty: lattice coincidences in the Protein Data Bank.

Acta crystallographica. Section D, Structural biology·2026

Same journal

Scotty: lattice coincidences for macromolecular crystallographic phasing.

Acta crystallographica. Section D, Structural biology·2026

Same journal

Miroslav Z. Papiz (1955-2026).

Acta crystallographica. Section D, Structural biology·2026

Same journal

Structural basis of regioselective double halogenation of the β-carboline tryptoline by the single-component halogenase AetF.

Acta crystallographica. Section D, Structural biology·2026

Same journal

Simulating neutron protein crystallography experiments: applications to the development of the NMX instrument at ESS.

Acta crystallographica. Section D, Structural biology·2026

Same journal

Molecular architecture of the human citrate synthase-malate dehydrogenase 2 metabolon.

Acta crystallographica. Section D, Structural biology·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Nov 22, 2025

High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE

High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE

Published on: May 16, 2017

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

Montserrat Fàbrega-Ferrer¹, Ana Cuervo², Francisco J Fernández³

¹Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028 Barcelona, Spain.

Acta Crystallographica. Section D, Structural Biology

|January 6, 2021

Summary

This summary is machine-generated.

Medium-resolution cryo-electron microscopy maps can aid in solving complex protein structures when other methods fail. This study demonstrates building a partial model from a cryo-EM map to determine a bacteriophage portal structure.

Keywords:

bacteriophage portal cryo-EM density modification molecular replacement

More Related Videos

Cryo-EM and Single-Particle Analysis with Scipion

Cryo-EM and Single-Particle Analysis with Scipion

Published on: May 29, 2021

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps

Published on: July 19, 2024

Related Experiment Videos

Last Updated: Nov 22, 2025

High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE

High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE

Published on: May 16, 2017

Cryo-EM and Single-Particle Analysis with Scipion

Cryo-EM and Single-Particle Analysis with Scipion

Published on: May 29, 2021

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps

Published on: July 19, 2024

Area of Science:

Structural Biology
Biophysics
Biochemistry

Background:

Medium-resolution cryo-electron microscopy (cryo-EM) maps, especially those rich in alpha-helices, can facilitate the construction of partial models.
These partial models are valuable for molecular replacement (MR) searches in crystallography when homologous structures are unavailable or experimental phasing methods have not succeeded.

Purpose of the Study:

To demonstrate the utility of building partial models from medium-resolution cryo-EM data for structure determination.
To present a case study of solving a bacteriophage portal structure using this approach.

Main Methods:

Building a partial 30% model into a 7.8 Å resolution cryo-EM map.
Utilizing the self-rotation function to ascertain the correct oligomerization state.
Applying density modification procedures incorporating rotation matrices and a mask derived from the cryo-EM structure.

Main Results:

Successfully solved the structure of a bacteriophage portal using a partial model derived from cryo-EM data.
Demonstrated the effectiveness of self-rotation function analysis for determining oligomeric states.
Highlighted the critical role of density modification in structure solution.

Conclusions:

A workflow utilizing partial models from medium-resolution cryo-EM maps can be a viable strategy for solving challenging crystallographic structures.
This method offers an alternative when traditional molecular replacement or experimental phasing fails.
The described strategy is potentially applicable to similar structural biology problems.