Table 2.

X-ray crystallography data collection and refinement statistics for CTX-M-14 mutant enzymes^a.

Data collection	P167S 5TWDb	E166A/P167S 5VTH	S70G/P167S/CAZ 5TWE	E166A/P167S/CAZ 5TW6	E166A/CAZ 5U53
Space group	P 32 2 1	P 32 2 1	P 32 2 1	P 32 2 1	P 41 21 2
a,b,c (Å)	41.6, 41.6, 231.9	41.7, 41.7, 233.1	41.6, 41.6, 232.2	41.5, 41.5, 231.2	42.0, 42.0, 262.9
α,β,γ (°)	90.0, 90.0, 120.0	90.0, 90.0, 120.0	90.0, 90.0, 120.0	90.0, 90.0, 120.0	90.0, 90.0, 90.0
Resolution Range (Å)	30.60 - 1.70 (1.79-1.70)	30.69 – 2.20 (2.28-2.20)	30.62 -1.50 (1.58 -1.50)	77.05 -1.70 (1.76 -1.70)	30.33 -1.40 (1.48 -1.40)
R-merge (%)	5.3 (12.0)	13.3 (31.1)	12.2 (26.6)	9.2 (50.9)	14.4 (98.4)
Rpim (%)	1.6 (3.5)	7.0 (15.1)	4.3 (7.9)	5.2 (28.1)	3.8 (24.9)
I/sigma	30.6 (16.5)	6.1 (3.4)	13.4 (7.9)	7.2 (2.3)	11.0 (2.9)
CC(1/2)	1.0 (1.0)	1.0 (1.0)	1.0 (1.0)	1.0 (0.8)	1.0 (0.9)
Multiplicity	11.9 (12.5)	2.0 (2.0)	2.0 (2.0)	4.7 (5.0)	2.0 (2.0)
Completeness (%)	100 (100)	95 (98)	100 (100)	100 (100)	98 (99)
Wilson B-factor (Å2)	12.93	23.31	14.2	17.5	11.3
No. of unique reflections	26936 (2641)	12217 (1195)	38791 (3790)	26575 (2595)	47186 (4664)
Refinement
R-work/R-free (%)	21.0/23.8	22.0/26.9	15.1/16.9	17.9/22.16	17.0/19.5
No. of protein residues	260	261	262	259	261
No. of water molecules	266	146	324	248	328
Ramachandran
Favored (%)	98	97	98	98	98
Outliers (%)	0	0	0	0	0
RMS deviations
Bond length (Å)	0.01	0.008	0.007	0.009	0.01
Bond angles (°)	0.98	0.82	1.49	0.96	1.12
Average B-factor (Å2)	24.8	36.1	22.2	27.4	16.5
Protein	24.1	36.2	19.9	26.1	14.0
Ligand	-		52.2	29.7	23.1
Solvent	30.3	34.0	33.6	37.0	30.9

^aValues in parentheses in the body of the table indicate highest resolution shell.

^bProtein data bank code for the deposited structure (PDB ID).