Table 1.

X-ray data collection and refinement statistics

	Tne2tox –Tni2 (selenomethionine)
Data collection
Beamline	21-ID-F
Wavelength (Å)	0.979
Space group	C2
Cell dimensions
a, b, c (Å)	176.7, 40.6, 95.9
α, β, γ (°)	90.0, 97.2, 90.0
Resolution (Å)	68.94–1.71 (1.77–1.71)a
Total no. of reflections	145,128
Total no. of unique reflections	72,673
Rmerge (%)b	5.4 (64.6)a
I/σI	13.8 (1.2)a
Completeness (%)	98.7 (89.4)a
Redundancy	2.0 (2.0)a
Refinement
Rwork/Rfree (%)c	18.1/21.6
No. of atoms
Protein	4236
Water	574
Average B-factors (Å2)
Protein	31.6
Water	40.6
r.m.s.d.
Bond lengths (Å)	0.007
Bond angles (°)	0.89
Ramachandran plot (%)d
Total favored	98.1
Total allowed	100.0
Coordinate error (Å)e	0.23

^a Values in parentheses correspond to the highest resolution shell.

^b R_merge = Σ Σ |I(k) − 〈I〉|/Σ I(k), where I(k) and 〈I〉 represent the diffraction intensity values of the individual measurements and the corresponding mean values. The summation is over all unique measurements.

^c R_work = Σ ‖F_obs| − k|F_calc‖/|F_obs|, where F_obs and F_calc are the observed and calculated structure factors, respectively. R_free is the sum extended over a subset of reflections (5%) excluded from all stages of the refinement.

^d Data were calculated using MOLPROBITY (49).

^e Maximum-likelihood based coordinate error was determined by PHENIX (50).