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. Author manuscript; available in PMC: 2016 Mar 1.

Published in final edited form as: Nat Struct Mol Biol. 2015 Aug 3;22(9):672–678. doi: 10.1038/nsmb.3064

Table 1.

Crystallographic data collection and refinement statistics.

	TNT-IFT Crystal form 1	TNT-IFT Crystal form 2
Data collection
Space group	P2₁2₁2₁	P2₁2₁2₁
Cell dimensions
a, b, c (Å)	70.6, 86.2, 62.6	75.3, 85.3, 63.2
α, β, γ (°)	90.0, 90.0, 90.0	90.0, 90.0, 90.0
Wavelength (Å)	0.97	0.97
Resolution (Å)	20-1.10 (1.14-1.10)	20-1.9 (1.97-1.90)
R _sym	5.7 (50.2)	7.2 (33.5)
I / σI	29.5 (4.5)	66.6 (10.8)
Completeness (%)	90.8 (55.5)	99.5 (93.3)
Redundancy	12.6 (8.8)	13.2 (9.7)
Refinement
Resolution (Å)	1.0-1.1	20-1.9
No. reflections	133,725	32,610
R_work / R_free	12.8 / 14.3	17.0 / 20.8
No. atoms
Protein	2,990	2,889
Water	506	461
B-factors (Å²)
Protein (TNT/IFT)	13.6 / 15.2	25.5 / 26.4
Water	29.9	36.1
R.m.s deviations
Bond lengths (Å)	0.006	0.008
Bond angles (°)	1.09	1.19

^*

Values in parentheses are for highest-resolution shells.