6ATG

Insights to complement factor H recruitment by the borrelial CspZ protein as revealed by structural analysis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2013-10-12
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.0
Spacegroup name	P 1 21 1
Unit cell lengths	43.742, 53.772, 116.587
Unit cell angles	90.00, 92.99, 90.00

Refinement procedure

Resolution	39.500 - 1.800
R-factor	0.1788
Rwork	0.178
R-free	0.20690
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2uwn 4cbe
RMSD bond length	0.007
RMSD bond angle	0.760
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	PHENIX (1.12_2829)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	43.700	1.790
High resolution limit [Å]	1.800	1.750
Rmerge	0.116
Number of reflections	53908	3570
<I/σ(I)>	6.1	2.5
Completeness [%]	98.0	99.4
Redundancy	4.1	3.8
CC(1/2)	0.991	0.914

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.8	293	200 mM MgCl2, 100mM Tris-HCl (pH 7.8), and 22-24% (w/v) PEG 3350