5CFV

Fusion of Maltose-binding Protein and PilA from Acinetobacter nosocomialis M2

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-B
Synchrotron site	APS
Beamline	23-ID-B
Temperature [K]	100
Detector technology	CCD
Collection date	2015-06-28
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.034
Spacegroup name	C 1 2 1
Unit cell lengths	173.883, 55.334, 49.670
Unit cell angles	90.00, 91.52, 90.00

Refinement procedure

Resolution	29.440 - 1.800
Rwork	0.182
R-free	0.22800
Structure solution method	MOLECULAR REPLACEMENT
Data reduction software	XDS
Data scaling software	Aimless (0.5.9)
Phasing software	PHASER (2.5.6)
Refinement software	PHENIX (1.9-1692)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	29.440	29.440	1.840
High resolution limit [Å]	1.800	9.010	1.800
Rmerge	0.047	0.030	0.480
Rpim	0.029	0.019	0.386
Total number of observations	151005	1263	5010
Number of reflections	42472
<I/σ(I)>	15.4	37.9	1.8
Completeness [%]	97.0	96	77.1
Redundancy	3.6	3.4	2.5
CC(1/2)	0.998	0.997	0.799

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	298	Drops were set at a ratio of 2:1 mother-liquor to protein, at 10mg/ml protein concentration. The mother-liquor consisted of 0.1M Bicine/Trizma pH 8.0, 0.06M MgCl2, 0.06M CaCl2, 25% MPD, 25% PEG3350, 25% PEG400