TABLE 2.

Data collection and refinement statistics

Values in parenthesis are for the highest resolution shell.

	Se-Met YafQ-DinJ	YafQ-DinJ native	Se-Met YafQ (H87Q)	WT YafQ	YafQ (H87Q)
Data collection
Wavelength (Å)	0.9791	1.0	0.9792	1.0	1.0
Space group	C2	C2	I23	C2221	P1
Unit-cell parameters	a = 175.31 Å, b = 119.79 Å, c = 119.72 Å, β = 130.11°	a = 175.90 Å, b = 120.25 Å, c = 120.20 Å, β = 130.40°	a = b = c = 125.45 Å	a = 41.30Å, b = 89.83Å, c = 75.02Å	a = 41.84Å, b = 42.49Å, c = 43.28Å, α = 109.93°, β = 106.12°, γ = 102.07°
Resolution (Å)	2.50 (2.54-2.50)a	2.10 (2.14-2.10)	3.00 (3.05-3.00)	1.50 (1.53-1.50)	1.50 (1.53-1.50)
Unique reflections	64,984 (3233)	111,791 (5575)	6735 (339)	22,814 (1104)	39,481 (1853)
Completeness (%)	99.9 (100)	99.9 (100)	100 (100)	100 (100)	96.3 (92.9)
Redundancy	7.5 (7.5)	4.9 (5.0)	29.9 (30.3)	10.0 (6.9)	3.9 (2.4)
Mean I/σ(I)	45.41 (10.52)	32.98 (9.32)	27.21 (11.04)	72.47 (16.23)	45.35 (8.25)
Molecules in asymmetric unit	16	16	2	1	2
Rmerge (%)	13.2 (44.4)	10.2 (45.8)	20.7 (47.6)	6.2 (16.7)	4.8 (12.2)
Structure refinement
Resolution range (Å)		43.71–2.10		28.79–1.50	26.26–1.50
Rwork/Rfree (%)		17.68/21.51		17.64/18.92	16.48/18.87
Average B factor (Å2)
Main chain		23.10		11.95	12.38
Side chain		27.59		16.10	15.89
Ligand (SO42−)		36.07		25.71	30.29
Waters		31.80		31.58	28.57
No. of atoms
Residues		1387		90	181
Protein		11,148		769	1532
Ligand (SO42−)		42		5	5
Waters		1223		217	430
Ramachandran plot (%)
Most favored		99.56		98.89	98.88
Allowed		0.44		1.11	1.12
Root mean square deviations
Bond lengths (Å)		0.008		0.006	0.005
Bond angles (degrees)		1.063		1.084	1.112

^a Values in parentheses are for the highest resolution shell.