Table 2.

Data collection and refinement statistics of mini-TrpRS complexed with Trp-AMP.

Data collection
Space group	C2
a=, Å	134.7
b=, Å	96.5
c=, Å	97.1
β=, °	129.9
Wavelength, Å	0.9116
Resolution, Å	2.0
Unique reflections	64590
Completeness, %*	99.5 (99.6)
Redundancy	7.3
Rmerge, %* †	3.8 (58.7)
<I/σ(I)>*	34.7 (2.0)
Refinement statistics
Resolution range, Å	20-2.0
Rwork / Rfree, %‡	25.35 / 29.75
rms deviation bond lengths, Å	0.007
rms deviation bond angle, °	1.3
Ramachandran plot, %
Favored	90.1
Allowed	8.8
generously allowed	1.0
disallowed	0.2
Average B-factors for protein, Å2	50.9
Average B-factors for substrate, Å2	53.5
Average B-factors for waters, Å2	42.5

^*Numbers in parentheses refer to the highest resolution shell.

^†R_merge = (Σ_hΣ_i|I_i(h)−<I(h)>|/Σ_hΣ_iI_i(h)) × 100, where <I(h)> is the average intensity of I symmetry-related observations of reflections with Bragg index h.

^‡R_work = (Σ_hkl|F_o−F_c|/Σ_hkl |F_o|) × 100, where F_o and F_c are the observed and the calculated structure factors, respectively, for 95% of the reflections used in the refinement. R_free was calculated as for R_work but on 5% of reflections excluded before refinement.