5OF2

The structural versatility of TasA in B. subtilis biofilm formation

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	BESSY BEAMLINE 14.1
Synchrotron site	BESSY
Beamline	14.1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2015-07-25
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.91841
Spacegroup name	P 1 21 1
Unit cell lengths	41.658, 43.039, 51.693
Unit cell angles	90.00, 90.17, 90.00

Refinement procedure

Resolution	41.658 - 1.860
R-factor	0.1747
Rwork	0.173
R-free	0.21180
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5of1
RMSD bond length	0.007
RMSD bond angle	0.988
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHASER
Refinement software	PHENIX (1.9_1692)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	41.660	1.920
High resolution limit [Å]	1.860	1.860
Rmerge	0.083	0.745
Number of reflections	15615	1542
<I/σ(I)>	13.83	1.85
Completeness [%]	99.6	97.84
Redundancy	4.5	4.4
CC(1/2)	0.998	0.804

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.8	293.15	34% PEG 2000 MME, 0.1M ammonium sulfate, 0.1M sodium acetate pH 4.8