Extended Data Fig. 7: The stalks of RS1 and RS2.
From: Structures of radial spokes and associated complexes important for ciliary motility

a, The stalk of the isolated radial spoke is consistent with the on-doublet stalk of RS1 only. FAP253, RSP14, and calmodulin are present in the stalk of RS1 but not RS2. RSP8, RSP15, and an unidentified ubiquitin (Ub)-like domain are present in the stalk of RS2 but not RS1. LC8, FAP207, and RSP3 are common to both RS1 and RS2 but adopt different conformations. The RSP7/11 heterodimer is similar in both radial spokes. b, RSP14 and RSP8 are structurally similar armadillo proteins present in different radial spokes. Left, RSP14 was identified in the stalk of RS1 based on well-defined sidechain density. Middle, the model of RSP14 is incompatible with the density of the armadillo protein in RS2, indicating that they are different proteins with similar folds. Right, a model for RSP8 built into the RS2 density. c, Superposition of the atomic models for RSP8 and RSP14.