Figure 6
From: Molecular structure and function of myelin protein P0 in membrane stacking
Full-length P0 in a membrane environment. (a) Cryo-EM of full length P0 displays good monodispersity in 0.4% DM. (b) SCRD spectra of full length P0 in detergents and lipids. (c) Analysis of full-length P0 monodispersity and oligomeric state using SEC-MALS. Shown are data measured in DPC. The Rayleigh ratio is shown (black) together with the total mass (gray dash), protein mass (red) and detergent mass for each peak (gray solid). (d) P0 reconstituted into DOPC and E. coli polar lipid extract vesicles result in membrane stacks that resemble myelin. (e) Cryo-EM micrographs of E. coli polar lipid extract with reconstituted P0. Both curved loosened and planar tight bilayer adhesions are present. In the latter, a significantly higher protein density between the membranes is evident. The loose and tight areas are marked with red arrows and white asterisks, respectively. (f) 2D class averages generated from the tight adhesions of P0 in E. coli polar lipids sample cryo-EM micrographs display a zipper of apposing Ig-like domains that interact with each other and settle between the two lipid bilayers.
