X-ray and Cryo-electron Microscopy Structures of Monalysin Pore-forming Toxin Reveal Multimerization of the Pro-form
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Aerolysin, a virulence factor secreted by Aeromonas hydrophila, is representative of a group of beta-sheet toxins that must form stable homooligomers in order to be able to insert into biological membranes and generate channels. Electron microscopy and ima ...
Aquaporins are transmembrane water channel proteins, which play important functions in the osmoregulation and water balance of microorganisms, plants, and animal tissues. All aquaporins studied to date are thought to be tetrameric assemblies of four subuni ...
Aerolysin is a channel-forming toxin that must oligomerize in order to become insertion-competent. Modeling based on the crystal structure of the proaerolysin dimer and electron microscopic images of the oligomer indicated that a loop in domain 3 must move ...
Aquaporins form a large family of membrane channels involved in osmoregulation, Electron crystallography has shown monomers to consist of six membrane spanning a-helices confirming sequence based predictions. Surface exposed loops are the least conserved r ...
ZnO and AlN, which exhibit the wurtzite structure, were deposited onto metal coated SiO2 substrates by sputtering. X-ray diffraction (XRD) indicated that the films contained no second phases and exhibited an [0001] texture. Transmission electron microscopy ...
The receptor that mediates the specific uptake and intracellular transport of dimeric immunoglobulin A (IgA dimer) in mucosal and glandular epithelia is identical with a transmembrane precursor of secreted secretory component. During transport, the IgA dim ...
Electron crystallography of membrane proteins uses cryo-transmission electron microscopy to image frozen-hydrated 2D crystals. The processing of recorded images exploits the periodic arrangement of the structures in the images to extract the amplitudes and ...
