Extended Data Fig. 4: Cryo-EM data analysis of the apo-OsSPS3–FBN5 complex.
From: Structural insights into the molecular mechanisms of OsFBN5-induced OsSPS3 catalysis
a, Anion exchange chromatography and SDS‒PAGE analysis of 3 peaks. Peak 1 corresponds to the apo-OsFBN5 (black), peak 2 represents the OsSPS3–FBN5 complex (blue), and peak 3 contains apo-OsSPS3 (light brown). Each corresponding band is labelled. This experiment was independently repeated three times with similar results. b, Representative negative staining images. The black arrows indicate the complex particles. Scale bar, 100 nm. This experiment was independently repeated three times with similar results. c, Flow chart for cryo-EM data analysis of the apo-OsSPS3–FBN5 complex. d, FSC curves for the apo-OsSPS3–FBN5 complex. e, Map of the apo-OsSPS3–FBN5 complex is colored according to estimated local resolution. f, Sample maps of N-terminal subdomains (helices A, B and C), dimerization interface (helices G and H), loops I, II, and III and the interaction interface of the apo-OsSPS3–FBN5 complex.
