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. 2012 Oct 10;20(10):1670–1680. doi: 10.1016/j.str.2012.07.003

Figure 3.

Figure 3

Architecture of the Primed Dynein Head

(A) Cryo-EM reconstruction of the dynein-c head in the ADP.Vi state, with the variance map overlaid (magenta wire mesh). The base of the linker is colored magenta. The resolution of the map is 22 Å according to the 0.5 FSC criterion (Figure S1A).

(B) Cryo-EM reconstruction of the cytoplasmic dynein head, bearing a E2027Q substitution, in the ATP state. Mean primed and unprimed locations of a GFP tag on the motor N terminus are indicated (solid and faded magenta spheres, respectively) (Roberts et al., 2009). The resolution of the map is 25 Å according to the 0.5 FSC criterion (Figure S1D).

(C) Cryo-EM class averages of ADP.Vi-dynein-c showing variation in the site of tail emergence from the head (black arrows, primed position; white arrows, unprimed position). Scale bar is 10 nm.