Supplementary Figure 4: Resolution of the cryo-EM density map and conformational changes of the 50S subunit upon HflX binding.
From: HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions
(a) Gold-standard Fourier Shell Correlation (FSC) curve. When FSC is 0.143, resolution of cryo-EM density map of the 50S–HflX–GMPPNP complex is 4.5 Å. (b) Local-resolution map of the cryo-EM map. (c) Histogram of local resolution in terms of individual voxels. (d) The atomic model of the 50S–HflX–GMPPNP complex is displayed in cartoon representation (rRNA colored marine and r-proteins colored green as above), superimposed with the model of the 50S subunit from a crystal structure of empty 70S ribosome (PDB id: 2AWB) (rRNA colored red and r-proteins colored yellow)1. (e-j) Close-up views of the local conformational changes on respective rRNA helices as boxed in d. The displacements of the helices upon HflX binding are marked with arrows.
