Table 2.

Data collection and refinement statistics.

	AtMTAN1-SAH
Diffraction statistics
Space group	P21
Unit cell dimensions (Å)
a	45.9
b	126.4
c	83.8
β (°)	101.7
No. observed reflections	173,922
No. unique reflections	46,037
Resolution range (Å)	23.12–2.20
Rmerge(%)a	8.4 (28.9)
Redundancy	3.8
Completeness (%)	97.2 (95.2)
Average (I/σI)	7.4 (3.0)
Refinement statistics
No. of protein atoms	7524
No. of ligand atoms	68
No. of water molecules	519
Resolution range (Å)	23.12–2.20
No. reflections in test set	4627
Test set size (%)	10
Rcryst(%)b	20.8
Rfree(%)c	26.2
Overall B factor (Å2)	22.6
Ligands	20.0
Water	23.1
R.m.s. deviation
Bonds (Å)	0.012
Angles (°)	1.4
Dihedral angles (°)	24.5
Improper angles (°)	3.0
Molprobity output scores (%)e
Ramachandran favored	98.1
Ramachandran outliers	0.0
Cruickshank’s DPI based on Rfreed	0.26

Values given in parentheses refer to reflections in the outer resolution shell: (2.28–2.20 Å).

^aR_merge = ΣΣ| I(k) − 〈I〉|/ΣI(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.

^b $R_{\text{cryst}}=\frac{\sum \mid \mid F_{\text{obs}}\mid -k\mid F_{\text{calc}}\mid \mid }{\sum \mid F_{\text{obs}}\mid }$, where F_obs and F_calc are the observed and calculated structure factors, respectively.

^cR_free is the sum extended over a subset of reflections (10%) excluded from all stages of the refinement.

^dCruickshank’s diffraction component precision index (DPI) as an estimate of coordinate error (Cruickshank, 1999).

^eAs calculated using Molprobity (Lovell et al., 2003).