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Related Concept Videos

Cryo-electron Microscopy01:28

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...
Determination of Crystal Structures01:29

Determination of Crystal Structures

In the late 1800s, the revelation that light extended beyond visible wavelengths led to the discovery of X-rays by Wilhelm Roentgen. Recognized as high-energy electromagnetic radiation with short wavelengths, X-rays prompted exploration into their interaction with crystals. Max von Laue proposed in 1912 that the periodic arrangement of atoms, ions, or molecules in crystals would cause them to diffract X-rays, a hypothesis confirmed through experiments with copper sulfate and zinc sulfide...
Electron Microscope Tomography and Single-particle Reconstruction01:07

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...

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Related Experiment Video

Updated: May 22, 2026

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

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

Published on: March 5, 2017

Membrane protein structure determination by electron crystallography.

Iban Ubarretxena-Belandia1, David L Stokes

  • 1Department of Structural and Chemical Biology, Mt. Sinai School of Medicine, New York, NY 10029, United States.

Current Opinion in Structural Biology
|May 11, 2012
PubMed
Summary
This summary is machine-generated.

Electron crystallography advances membrane protein structure determination, revealing transporter mechanisms and lipid interactions. Technical improvements enhance high-throughput screening and automated imaging for faster structure elucidation.

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Last Updated: May 22, 2026

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
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Published on: March 5, 2017

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases
22:00

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases

Published on: November 21, 2010

Assessing Two-dimensional Crystallization Trials of Small Membrane Proteins for Structural Biology Studies by Electron Crystallography
09:23

Assessing Two-dimensional Crystallization Trials of Small Membrane Proteins for Structural Biology Studies by Electron Crystallography

Published on: October 29, 2010

Area of Science:

  • Structural biology
  • Biophysics
  • Membrane protein research

Background:

  • Electron crystallography is a key technique for determining the 3D structure of membrane proteins.
  • Understanding membrane protein mechanisms requires high-resolution structural data.
  • Interactions between membrane proteins and lipids are crucial for function.

Purpose of the Study:

  • To summarize recent advancements in electron crystallography of membrane proteins.
  • To highlight new insights into transporter mechanisms and lipid interactions.
  • To review technical and computational developments facilitating structure determination.

Main Methods:

  • Application of electron crystallography to membrane protein systems.
  • High-throughput screening of crystallization trials.
  • Automated imaging using electron microscopy.
  • Development of novel software and computational methods (e.g., molecular replacement, phase extension).

Main Results:

  • Structural insights into the mechanisms of various transporters.
  • Detailed understanding of membrane protein-lipid interactions within the bilayer.
  • Significant progress in high-throughput screening and automated data acquisition.
  • Improved computational tools for accelerating structure determination.

Conclusions:

  • Electron crystallography continues to yield crucial structural information on membrane proteins.
  • Recent technical and computational innovations are making structure determination more efficient.
  • These advances are vital for understanding transporter function and protein-lipid dynamics.