Fig. 4: Cryo-EM of CHMP1B F9 and F13 double mutants with SDPC-Br (lipid composition 10).
From: Brominated lipid probes expose structural asymmetries in constricted membranes
a–d, A section of CHMP1B helix α1 atomic model (PDB 6TZ5) and cryo-EM density (gray) for WT CHMP1B (a) and double mutant proteins, CHMP1B F9A/F13A (b), CHMP1B F9L/F13L (c) and CHMP1B F9E/F13E (d). e–h, Horizontal (top) and vertical (middle) slices through the cryo-EM densities for the CHMP1B WT (e) and CHMP1B double mutant proteins, CHMP1B F9A/F13A (f), CHMP1B F9L/F13L (g) and CHMP1B F9E/F13E (h). The bottom panels show enlarged images of the membrane-contact sites for each sample. Small and polar side chains induce elastic deformations in the bilayer, while hydrophobic side chains induce hydrophobic defects.
