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. 2019 Apr 15;2:131. doi: 10.1038/s42003-019-0365-y

Table 2.

Data collection and refinement statistics

	PpArsN1^a	PpArsN1-AST^a	PpArsN1-PPT^a
Data collection
Space group	P4₃2₁2	C121	P12₁1
Cell dimensions
a, b, c (Å)	67.02, 67.02, 206.74	185.27, 141.74, 54.55	53.84, 142.69, 178.31
α, β, ϒ (°)	90.0, 90.0, 90.0	90.0, 90.6, 90.0	90, 89.9, 90.0
Resolution (Å)	30.64–2.16 (2.20–2.16)^b	50.00–2.19 (2.23–2.19)^b	39.91–2.66 (2.75–2.66)^b
R _merge	0.078 (0.342)^b	0.150 (0.654)^b	0.157 (1.144)^b
I/ σ I	6.9 (2.9)^b	12.4 (1.9)^b	11.0 (1.9)^b
Completeness (%)	97.6 (90.8)^b	99.4 (95.7)^b	97.0 (97.2)^b
Redundancy	5.16 (4.31)^b	7.3 (4.4)^b	4.2 (3.9)^b
Refinement
Resolution (Å)	30.64–2.16 (2.24–2.16)^b	49.02–2.19 (2.24–2.19)^b	39.91–2.66 (2.69–2.66)^b
No. of reflections	25,795	67,549	70,774
R_work/R_free	0.237/0.266	0.180/0.232	0.224/0.272
No. of atoms
Protein	2681	8443	15,829
Ligand/ion	-	26	89
Water	104	874	222
B-factors
Protein	34.95	29.97	39.49
Ligand/ion	-	41.66	55.00
Water	38.10	35.12	37.89
R.m.s. deviations
Bond lengths (Å)	0.004	0.013	0.004
Bond angles (˚)	0.905	1.477	0.880

^aEach structure was refined from a single data set from an independent protein crystal

^bValues in parentheses are for highest resolution shell