Extended Data Fig. 1: Endogenous purification of the DGC from mouse skeletal muscle.
From: Structure and assembly of the dystrophin glycoprotein complex
a, A classic schematic showing the overall organization of the DGC. The LG4 and LG5 domains of laminin-α2 interact with the glycans on α-DG. Inset: crystal structure of the LG4 and LG5 domains of laminin-α2 in complex with glycans (PDB: 5IK5). ECM: extracellular matrix; ABD: actin-binding domain; CR: cysteine-rich domain; CT: C-terminal domain. b, Size-exclusion chromatogram and corresponding SDS-PAGE analysis of the purified LG4 and LG5 domains of laminin-α2. Purifications were repeated independently at least three times with similar results. c, A diagram showing the purification procedure of the native DGC from mouse skeletal muscle. SEC: size exclusion chromatography; WB: western blot; MS: mass spectrometry. d, Size exclusion chromatography profile of the purified DGC sample. The shaded fractions were collected for cryo-EM and MS analysis. e, Western blot analysis of the gel filtration fractions against multiple DGC components. Each western blot was repeated at least twice with similar results. For gel source data, see Supplementary Fig. 1a. f, MS analysis of the purified DGC sample. Potential DGC components are listed in the order of decreasing peptide-spectrum match (PSM) scores. The DGC components observed in our model are highlighted in green. g, Peptide identification of dystrophin by MS analysis of the purified DGC sample. The identified regions are shaded in cyan, which account for a total of 67% sequence coverage.
