28LI

Crystal structure of complement-inhibiting protein ChiA of Borrelia recurrentis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SLS BEAMLINE X10SA
Synchrotron site	SLS
Beamline	X10SA
Temperature [K]	100
Detector technology	PIXEL
Collection date	2021-05-17
Detector	DECTRIS EIGER2 XE 16M
Wavelength(s)	1.0
Spacegroup name	C 1 2 1
Unit cell lengths	53.070, 115.840, 83.030
Unit cell angles	90.00, 90.03, 90.00

Refinement procedure

Resolution	48.250 - 2.710
R-factor	0.2578
Rwork	0.253
R-free	0.29920
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.004
RMSD bond angle	0.962
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHENIX
Refinement software	PHENIX (1.19.2_4158)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.250	2.807
High resolution limit [Å]	2.710	2.710
Number of reflections	13514	1343
<I/σ(I)>	13.47
Completeness [%]	98.3	95.77
Redundancy	6.5
CC(1/2)	0.999	0.782

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	8.5	277	sead bead method. Initial crystals sitting drop, 20% PEG400, 16% PEG4000, 70mM MgCl, 100mM Tris8.5 seed crystals hangig drop, 20%PEG400, 16%PEG4000, 50mM MgCl, 100mM Tris8.5