Table 2.

X-ray diffraction data of mutant OmpF porins

Data	Mutant
	S272A	E296A	E296L	E296Q	D312N	Δ116–120	E117C/A333C
X-ray source	ESRF	ESRF	Basel	ESRF	Basel	Basel	Basel
Resolution, Å*	2.1	2.4	2.5	2.8	2.2	3.1	3.0
No. of unique reflections	24,276	16,831	14,272	10,688	21,639	7,631	8,527
Rmerge, %	11.1	6.6	9.3	7.9	7.0	12.0	8.8
Completeness, %	91.4	98.4	96.6	97.6	97.6	95.8	96.8
Redundancy	1.8	3.3	5.5	2.9	7.6	3.0	2.5
R, %	21.0	17.7	18.7	18.5	20.3	22.4	18.6
Rfree, %	27.1	25.7	26.2	26.8	25.4	32.4	27.1
rms deviation†
Bond lengths, Å	0.018	0.017	0.014	0.009	0.019	0.012	0.008
Bond angles, °	0.043	0.044	0.041	0.034	0.043	0.044	0.031
rms deviation, mutant − wild type‡ Å	0.12	0.08	0.17	0.13	0.28	0.29	0.17

X-ray sources were a rotatory anode generator (Basel) or the Swiss–Norwegian beam line at the European Synchrotron Radiation Facility (ESRF) in Grenoble, France. All data were collected on Mar Research image plates. 

^*The low-resolution cutoff was 15 Å for all structures. 

^†rms deviation from ideal values. 

^‡rms deviation between all C^α positions of the mutant and wild-type model.