Table 1 Cryo-EM and refinement statistics

	FH^571–718F	FH^571–718F	FH^451–718F + KIF1CS^674–822	FH^451–718F + KIF1CS^674–922	FH^451–718F + KIF1CS^674–922
Electron Microscopy Data Bank ID	18302		18303	—	—
Protein Data Bank ID	8QAT		—	—	—
Data collection and processing
Magnification	81,000×	75,000×	81,000×	81,000×	81,000×
Voltage	300	300	300	300	300
Pixel size (Å)	1.059	1.09	1.059	1.059	1.059
Electron exposure (e⁻ Å⁻²)	44	34	44	43	54
Defocus range (μm)	1.6–2.6	1.6–2.6	1.6–2.6	1.3–2.7	1.3–2.7
Initial movies	26,383	16,446	11,839	5,726	7,424
Initial particle images	902,151	1,605,779	2,368,723	1,297,609	952,300
Final particle images	273,204			507,489	—
Symmetry imposed	C1	C1	C1	C1	C1
Map resolution (Å)	3.2^a			4.8^b
Fourier shell correlation threshold	0.143^a			0.143^b
Map-sharpening B factor (Å²)	−116.705^a			−10^b
Model refinement
Model resolution (Å)	3.52^a			—	—
Fourier shell correlation threshold	0.5^a			—	—
Model composition
Nonhydrogen atoms	7,758^a			—	—
Protein residues	970^a			—	—
Ligands	—			—	—
Mean B factors (Å²)
Protein	100.08^a			—	—
Ligand	—			—	—
Root mean square deviations
Bond lengths (Å)	0.006^a			—	—
Bond angles	1.267°^a			—	—
Validation
Clash score	3.47^a			—	—
MolProbity score	1.14^a			—	—
Rotamers outliers (%)	0.35^a			—	—
Ramachandran plot
Favored (%)	98.01^a			—	—
Allowed (%)	1.89^a			—	—
Outliers (%)	0.1^a			—	—

^aValue obtained from three merged datasets. ^bValue obtained from two merged datasets.

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