9XVH

Crystal structure of mature Bacteroides fragilis toxin 1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRF BEAMLINE BL02U1
Synchrotron site	SSRF
Beamline	BL02U1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2025-04-20
Detector	DECTRIS EIGER2 S 9M
Wavelength(s)	0.97918
Spacegroup name	P 1
Unit cell lengths	55.318, 63.841, 65.170
Unit cell angles	90.29, 111.89, 111.72

Refinement procedure

Resolution	38.670 - 1.940
R-factor	0.2269
Rwork	0.225
R-free	0.26570
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	0.805
Data reduction software	autoPROC
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.20.1_4487)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	58.490	2.050
High resolution limit [Å]	1.940	1.940
Rmerge		1.061
Number of reflections	50986	6899
<I/σ(I)>	2.9	0.7
Completeness [%]	91.4
Redundancy	2.2
CC(1/2)	0.993	0.435

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	Crystals were grown from a crystallization solution containing 0.2 M sodium acetate trihydrate, 0.1 M sodium cacodylate pH 6.5 and 21% (w/v) PEG 8000. The protein solution was at a concentration of 20 mg/ml.