9RRT

Crystal structure of Borrelia recurrentis variable large protein VlpA1 (VmpA1)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I03
Synchrotron site	Diamond
Beamline	I03
Temperature [K]	100
Detector technology	PIXEL
Collection date	2024-11-28
Detector	DECTRIS EIGER2 XE 16M
Wavelength(s)	0.953738
Spacegroup name	P 21 21 21
Unit cell lengths	37.891, 77.723, 170.563
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	85.280 - 2.450
R-factor	0.20125
Rwork	0.197
R-free	0.27070
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.547
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	REFMAC (5.8.0267)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	170.560	2.550
High resolution limit [Å]	2.450	2.450
Rmerge	0.113
Number of reflections	18874	2171
<I/σ(I)>	13.8	5.5
Completeness [%]	97.3
Redundancy	13.1
CC(1/2)	0.997	0.967

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	294	22% Jeffamine ED-2001 3% PEG 3350