Fig. 2: Cryo-EM 3D density maps.

Iso-density surface representations of the twenty cryo-EM maps determined. The columns correspond to the four different nucleotide conditions used and the rows to the five KIF14 constructs used. Each panel shows two views of the MT-KIF14 3D map rotated 180° from each other (MT protofilament partially shown). Surfaces are colored according to the fitted atomic structure they enclose: α-tubulin in light gray, β-tubulin in dark gray, most of the kinesin motor domain in blue with the switch-1 loop in green, the switch-2 loop in magenta, KH0 in yellow, the bound nucleotide (ADP or AMP-PNP) in orange, the neck-linker in red, and the CC1 coiled coil in bright green. Closed or open refers to the deduced conformation of the motor domain. T and L indicate trailing or leading motor domains in the two-heads-bound dimer structures. Numbers between the K743 AMP-PNP and ADP-AlFx, open and closed structures indicate the relative population of each conformation (open or closed). Densities in the undocked neck-linker and coiled coil (only present in the K755 and K772 maps) are noisier than the rest of the map and are displayed at a lower contour level after low pass-filtration to 7–8 Å. The figure was prepared with VMD⁶⁹.