Extended Data Fig. 1: Biochemical analysis of the oligomeric assembly formed by CUL9–RBX1. | Nature Structural & Molecular Biology

Extended Data Fig. 1: Biochemical analysis of the oligomeric assembly formed by CUL9–RBX1.

From: Noncanonical assembly, neddylation and chimeric cullin–RING/RBR ubiquitylation by the 1.8 MDa CUL9 E3 ligase complex

Extended Data Fig. 1: Biochemical analysis of the oligomeric assembly formed by CUL9–RBX1.

a, Left: Size-exclusion chromatography profiles of recombinant CUL9-RBX1 (orange) and molecular weight standards (Bio-Rad, black) from a Superose 6, 5/150GL column. Right: Coomassie-stained SDS-PAGE analysis of peak fractions of CUL9-RBX1 (n = 2 technically independent experiments). b, C3-symmetric hexameric CUL9-RBX1 structure, showing the three constituent cullin dimer subcomplexes in different colors. c, Size exclusion chromatography-multiangle light scattering (SEC-MALS) of CUL9-RBX1 confirms hexameric assembly with roughly 1.8 MDa molecular weight. d, Coomassie-stained SDS-PAGE analysis of sucrose gradient fractionation of Bio-Rad molecular weight standards (n = 2 technically independent experiments). e, Close-up of CUL9-RBX1 hexamer structure overlaid with transparent cryo-EM density, focused on the N-terminal ARM1 dimerization interface.

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