Related Experiment Video

Updated: May 28, 2026

The Automated Crystallography Pipelines at the EMBL HTX Facility in Grenoble
06:50

The Automated Crystallography Pipelines at the EMBL HTX Facility in Grenoble

Published on: June 5, 2021

A helical processing pipeline for EM structure determination of membrane proteins

Lauren S Fisher1, Andrew Ward, Ronald A Milligan

  • 1The National Resource for Automated Molecular Microscopy, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

Methods (San Diego, Calif.)
|October 4, 2011
PubMed
Summary

Electron crystallography determines integral membrane protein structures using helical crystals. This study integrates standard Fourier-Bessel analysis into the Appion pipeline for streamlined 3D structure determination.

More Related Videos

A Robust Single-Particle Cryo-Electron Microscopy (cryo-EM) Processing Workflow with cryoSPARC, RELION, and Scipion13:43

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

Published on: January 31, 2022

Single Particle Cryo-Electron Microscopy: From Sample to Structure11:52

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Published on: May 29, 2021

Related Concept Videos

Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Detergent Purification of Membrane Proteins01:18

Detergent Purification of Membrane Proteins

Detergents are used to purify the integral proteins of the membrane. The hydrophobic portion of the detergent can replace membrane phospholipids while solubilizing the membrane proteins. When detergent monomers reach a specific concentration in a solution called critical micelle concentration (CMC), they form micelles. Above CMC, the concentration of the detergent monomers remains in equilibrium with the micelle. The number of detergent monomers present in the CMC varies for each detergent, and...