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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...

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Updated: Dec 29, 2025

The CryoAPEX Method for Electron Microscopy Analysis of Membrane Protein Localization Within Ultrastructurally-Preserved Cells

The CryoAPEX Method for Electron Microscopy Analysis of Membrane Protein Localization Within Ultrastructurally-Preserved Cells

Published on: February 27, 2020

Using MemBlob to Analyze Transmembrane Regions Based on Cryo-EM Maps.

Georgina Csizmadia^1,2, Bianka Farkas^1,2,3, Eszter Katona^1,4

¹Department of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary.

Methods in Molecular Biology (Clifton, N.J.)

|February 2, 2020

Summary

MemBlob is a new method using cryo-electron microscopy (cryo-EM) difference maps to determine the precise location of transmembrane proteins within cell membranes. This approach reveals which surface residues interact with the lipid bilayer.

Keywords:

Cryo-EM map Lipid interface Transmembrane region

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Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

Published on: January 7, 2019

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Last Updated: Dec 29, 2025

The CryoAPEX Method for Electron Microscopy Analysis of Membrane Protein Localization Within Ultrastructurally-Preserved Cells

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Published on: February 27, 2020

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Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

Published on: January 7, 2019

Area of Science:

Structural biology
Biochemistry
Membrane protein research

Background:

Transmembrane proteins are crucial for cell function but are less understood than soluble proteins.
Determining the exact position of transmembrane proteins within the lipid bilayer is experimentally challenging at the atomic level.

Purpose of the Study:

To introduce MemBlob, a novel computational approach for determining transmembrane protein positions.
To leverage cryo-electron microscopy (cryo-EM) data for precise localization of membrane proteins.

Main Methods:

Utilizing difference electron density maps from cryo-EM studies of transmembrane proteins.
Analyzing the non-protein regions of the maps to identify membrane mimetic localization.
Integrating protein structural models with experimental electron density maps.

Main Results:

MemBlob successfully estimates the positional information of transmembrane proteins within the lipid bilayer.
The method provides an estimation of surface residues that interact with the membrane.
Successfully extracts positional information from experimental data.

Conclusions:

MemBlob offers a new way to investigate transmembrane protein structure and localization.
This method enhances our understanding of membrane protein-lipid interactions.
The approach aids in characterizing the structural and positional aspects of membrane proteomes.