Fig. 6: Two mutations are necessary to form predominant dimer or monomer populations.
From: A domain-swapped CaMKII conformation facilitates linker-mediated allosteric regulation

A The dodecameric CaMKIIδ hub from the crystal structure presented here is shown with the kinase domains omitted for clarity. Residues highlighted on the right (F368, L405, Q407) are positioned in the lateral hub interface and on the bottom (C399 and H439) are positioned in the equatorial hub interface. B Mass photometry analyses at different concentrations of CaMKIIδ holoenzymes with mutations at either or both hub interfaces. Cartoon representations on the right show the positions of the mutations (indicated as X). The kinase domains are translucent for clarity. Data are represented as mean molecular weight ± SD, n = 3 technical replicates. Source data are provided in Supplementary Fig. 4.