Table 1.

Cryo-EM data collection, refinement and validation statistics

	Closed, consensus (EMD-12605) (PDB 7NVL)	Closed, tubulin-bound (EMD-12607) (PDB 7NVN)	Closed, Actin/PhLP2A-bound (EMD-12606) (PDB 7NVM)	Open (EMD-12608) (PDB 7NVO)	Open, Map-only (EMD-13754)
Data collection and processing
Magnification	81,000	81,000	81,000	81,000	81,000
Voltage (kV)	300	300	300	300	300
Electron exposure (e–/Å2)	62	62	62	62	62
Defocus range (μm)	0.75 to 2.5	0.75 to 2.5	0.75 to 2.5	0.75 to 2.5	0.75 to 2.5
Pixel size (Å)	1.06	1.06	1.06	1.06	1.06
Symmetry imposed	C2	C1	C1	C1	C1
Initial particle images (no.)	3,856,544	3,856,544	3,856,544	3,856,544	3,856,544
Final particle images (no.)	316,195	93,758	63,082	50,405	144,903
Map resolution (Å)	2.5	3.0	3.1	3.5	3.5
FSC threshold	0.143	0.143	0.143	0.143	0.143
Map resolution range (Å)	2.5–4.4	2.8–4.8	2.9–6.6	3.2–9.9	3.1–11.7
Map sharpening B factor (Å2)	-63.0	-65.3	−57.7	−70.2	−95.3
Refinement
Initial model used (PDB code)	6KS6	6KS6	6KS6	6NRA
Model-to-map resolution (Å)	2.64	3.05	3.27	3.51
FSC threshold	0.5	0.5	0.5	0.5
Model-to-map correlation (Phenix)	0.73	0.86	0.74	0.81
Model composition
Non-hydrogen atoms	66,477	69,139	71,009	34,246
Protein residues	8626	8970	9219	4480
Ligands	48	48	48	44
B factors (Å2)
Protein	72.62	72.55	70.77	64.35
Ligand	171.45	171.45	158.28	136.15
R.m.s. deviations
Bond lengths (Å)	0.007	0.004	0.008	0.005
Bond angles (°)	0.827	0.607	0.863	0.816
Validation
MolProbity score	1.64	1.77	1.85	2.07
Clash score	4.63	6.80	7.32	6.81
Poor rotamers (%)	1.73	1.75	1.55	1.87
Ramachandran plot
Favored (%)	96.57	96.69	95.6	92.01
Allowed (%)	3.33	3.22	4.29	7.81
Disallowed (%)	0.09	0.09	0.11	0.18