8EC3

The crystal structure of the complement inhibitory domain of Borrelia hermsii FbpC.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-BM
Synchrotron site	APS
Beamline	22-BM
Temperature [K]	93
Detector technology	CCD
Collection date	2021-11-29
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.0
Spacegroup name	P 1 21 1
Unit cell lengths	38.239, 46.557, 45.186
Unit cell angles	90.00, 110.80, 90.00

Refinement procedure

Resolution	31.280 - 1.500
R-factor	0.1792
Rwork	0.177
R-free	0.19980
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	AlphaFold
RMSD bond length	0.010
RMSD bond angle	1.053
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHENIX
Refinement software	PHENIX (1.19.2-4158)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	31.280	1.550
High resolution limit [Å]	1.500	1.500
Rmeas	0.087	0.509
Rpim	0.032	0.218
Number of reflections	23546	2109
<I/σ(I)>	19.4	2
Completeness [%]	98.7	89.2
Redundancy	7
CC(1/2)	0.989	0.870

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	298.15	Crystals were grown in the following condition containing 0.2M magnesium (II) chloride, 0.1M bis-tris (pH 5.5), and 25% PEG 3,350. Crystals were cryoprotected in a buffer containing 0.2M magnesium (II) chloride, 0.1M sodium citrate (pH 5.4), 25% PEG 3,350, and 10% glycerol.