Fig. 1: Structure of OLE homodimer.
From: Naturally ornate RNA-only complexes revealed by cryo-EM
a, Top, representative micrograph (6,752 micrographs total). Particles selected for reconstruction are circled in white. Bottom, 2D class averages. Scale bar, 50 nm. b, The cryo-EM reconstruction of the OLE dimer. The top left image depicts the separation of the two chains: one chain on the right and the other on the left. Each domain of both chains is coloured. To aid visualization, the flexible P9.3 domain (red) is displayed with the unsharpened map at 10σ contour. The proposed binding sites of previously described proteins (RpsU, OapC and OapA) are labelled. c, Secondary structure of OLE dimer. The domains are coloured as in b. d–f, The intermolecular bridge interactions B1 (d), B2 (e) and B3 (f), coloured by domain. In d, the domain colouring is darker for chain A to differentiate the chains. g, The kink-turn motif that may bind the OapC protein, identical for each monomer. The sharpened cryo-EM map is displayed at the following contours: 7σ (b), 15σ (d), 12σ (f) and 10σ (g).
