Projection structure of full length connexin 43 by electron cryo-crystallography
Anchi Cheng1, Daniel Schweissinger, Farah Dawood
1Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Abstract:
We previously used electron cryo-crystallography to determine the three-dimensional structure of recombinant gap junction channels formed by a C-terminal truncation mutant of Cx43 (11). The dodecameric channel is formed by the end-to-end docking of two hexameric connexons, each comprised of 24 transmembrane alpha-helices. We have now generated two-dimensional crystals of the recombinant, full-length channel, as well as crystals in which the C-tail has been completely removed by trypsin digestion. Projection density maps at 7.5 A resolution closely resemble our previous analysis of the C-terminal truncation mutant (9). A difference map between the full length and trypsin-treated channels suggests that there are small but significant shifts in protein density upon removal of the C-tail.
More Related Videos
09:25Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction
Published on: January 9, 2015
13:28High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE
Published on: May 16, 2017
Related Concept Videos
Electron Microscope Tomography and Single-particle Reconstruction
Electron Tomography
Electron tomography can be performed either in TEM or STEM (scanning transmission...
Cryo-electron Microscopy
X-ray Crystallography
Diffraction
Diffraction is the change in the direction of travel experienced by an electromagnetic wave when it encounters a physical barrier whose dimensions are comparable to those of the wavelength of the light. X-rays are electromagnetic radiation with wavelengths about as long as the distance between neighboring...
