Table 1. Data collection, phasing and refinement statistics.

	FolT1	AMP–PNP bound ECF–FolT2	apo ECF–FolT2
Data collection
Space group	C121	P1	P1
Cell dimensions
a, b, c (Å)	108.91, 77.54, 89.45	90.07, 97.26, 105.45	88.82, 95.32, 107.57
α, β, γ (°)	90.0, 116.36, 90.0	84.67, 64.78, 62.59	83.45, 65.75, 61.99
Resolution (Å)	43.0–3.01 (3.32–3.01)*	43.9–3.30 (3.40–3.30)*	49.0–3.00 (3.07–3.00)*
Rmerge	0.12 (0.38)*	0.026 (0.86)*	0.04 (0.92)*
I/σI	5.3 (2.18)*	12 (1.10)*	10.5 (1.65)*
Completeness (%)	82.3 (44)*	94.4 (78.8)*	92.6 (86.6)*
Redundancy	2 (1.8)*	1.8 (1.7)*	1.8 (1.72)*
Refinement
Resolution (Å)	3.01	3.30	3.00
No. of reflections	10,960	33,723	41,549
Rwork/Rfree	0.235/0.286	0.252/0.294	0.232/0.279
No. of atoms	2,456	15,554	15,398
Protein	2,392	15,430	15,398
Ligand/ion	64	124	—
Water	—	—	—
B-factors
Protein	36	159	98
Ligand/ion	17	158	—
Water	—	—	—
R.m.s. deviations
Bond lengths (Å)	0.011	0.006	0.005
Bond angles (°)	1.429	1.404	1.263

For each structure, one crystal was used for data collection.

^*Values in parentheses are for the highest-resolution shell.