Table 1.

X-Ray Data Collection and Refinement, AcrA(45-312)-4M

Data Collection
Beamline	APS-BM19			ALS-8.2.2
Data set	λ1	λ2	λ3	λ1
Wavelength (Å)	0.97938	0.97955	0.96415	1.0000
Resolution (Å)a	50-3.00 (3.11-3.00)	50-3.39 (3.59-3.39)	50-3.50 (3.63-3.50)	50-2.70 (2.77-2.70)
Completeness (%)	99.3 (99.3)	99.8 (99.9)	99.8 (99.9)	97.3 (91.1)
Redundancy	4.2 (3.4)	4.4 (4.5)	4.2 (3.8)	5.0 (3.9)
I/σ	13.5 (2.3)	16.6 (4.6)	12.0 (4.0)	14.6 (2.3)
Rmergeb	13.9 (76.1)	9.8 (38.9)	18.5 (53.4)	9.0 (42.9)

Phasing
	Se λ1	Se λ2	Se λ3
Anomalous and dispersive differences (%)c
Se λ1	4.2
Se λ2	1.8	2.4
Se λ3	2.0	3.8	3.1
Anomalous phasing powerd	1.5	0.8	0.7
Number of sites	16
Figure of merit (40-3.0 Å)	0.59

Refinement
Resolution	50.0-2.71 (2.77-2.71)
Rcryst (%)e	23.7 (40.8)	Rms deviation
Rfree (%)e	27.5 (47.4)	Bonded B factor (Å2)	3.30
Number of reflections		From ideal geometry
Working set	35,426	Lengths (Å)	0.010
Test set	1,873	Angles (°)	1.608
Number of atoms		Average B factors (Å2)
Protein	6936	Protein	89.2
Solvent	36	Solvent	64.0

^aHighest resolution shell is in parentheses.

^b

$${\mathrm{R}}_{\mathrm{merge}}=100\times \frac{{\sum }_h{\sum }_i\mid I_{h,i}-I_h\mid }{{\sum }_h{\sum }_i{I}_{h,i}}$$

, where I_h is the mean intensity of symmetry-related reflections, I_h,j.

^cAnomalous and dispersive differences = 100 × rms ΔF/rms F, where ΔF for anomalous differences is (F_+h - F_-h)/2 (diagonal element) and for dispersive differences is F_λi - F_λj (off-diagonal).

^dF_H″/E, with F_H″ being the anomalous component of the heavy atom structure factor and E the rms lack-of-closure error.

^e

$$R\mathrm{factor}=100\times \frac{{\sum }_{hkl}\mid F_{obs}-F_{calc}\mid }{{\sum }_{hkl}{F}_{obs}}$$

, where R_free is calculated for a randomly chosen 5% of reflections (F > 0) omitted from refinement, and R_cryst is calculated for the remaining 95% of reflections (F > 0) included in refinement.