Table 2.

Data collection and crystal structure refinement statistics

Crystal	d‐methionine bound Nm MetQ	l‐methionine bound Nm MetQ	Substrate‐free NmMetQ
Wavelength (å)	0.9794	0.9792	0.9794
Resolution range (å)	34.31–1.678 (1.738–1.678)	34.2–1.547 (1.602–1.547)	34.22–1.559 (1.615–1.559)
Space group	P 1	P 1	P 21 21 2
Unit cell (a b c (å), α β γ (°))	79.66, 87.93, 91.64, 114.83, 104.12, 105.39	79.58, 87.65, 91.63, 114.70, 104.41, 105.24	52.56, 89.66, 45.088
Total reflections	3,103,914 (143,999)	1,954,462 (86,262)	203,203 (7,841)
Unique reflections	219,472 (21,547)	277,550 (13,387)	30,754 (2,741)
Multiplicity	14.1 (13.9)	7.0 (6.4)	6.5 (5.4)
Completeness (%)	96.04 (91.50)	95.95 (93.74)	98.77 (89.75)
Mean I/sigma(I)	10.5 (0.7)	18.8 (1.7)	10.4 (2.4)
Wilson B‐factor (å2)	27.47	23.04	17.16
R‐merge	0.132 (4.454)	0.042 (0.906)	0.167 (3.329)
R‐meas	0.137 (4.635)	0.049 (1.086)	0.181 (3.692)
R‐pim	0.036 (1.249)	0.018 (0.422)	0.071 (1.551)
CC1/2	0.999 (0.294)	1 (0.723)	0.995 (0.182)
Reflections used in refinement	218,427 (20,806)	27,7,479 (27,097)	30,752 (2741)
Reflections used for R‐free	11,054 (954)	13,991 (1,396)	2,000 (179)
R‐work	0.177 (0.355)	0.162 (0.263)	0.188 (0.258)
R‐free	0.201 (0.366)	0.180 (0.296)	0.220 (0.291)
Number of non‐hydrogen atoms	12,841	13,172	2,143
Macromolecules	11,454	11,448	1,895
Solvent	1,387	1,724	248
Protein residues	1,451	1,452	241
RMS bonds (å)	0.010	0.005	0.003
RMS angles (°)	1.11	0.92	0.68
Ramachandran favored (%)	97.91	97.84	97.49
Ramachandran allowed (%)	2.09	2.09	2.51
Ramachandran outliers (%)	0.00	0.07	0.00
Rotamer outliers (%)	1.47	1.23	0.99
Clashscore	2.73	2.60	2.66
Average B‐factor (å2)	34.89	29.39	25.47
Macromolecules	33.95	27.78	24.52
Solvent	42.69	40.08	32.69
Number of TLS groups			4

Note: Statistics for the highest‐resolution shell are shown in parentheses.

Abbreviations: TLS, translation/libration/screw.