8ETF

Bile Salt Hydrolase B from Lactobacillus gasseri with covalent inhibitor bound

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-09-29
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	1.0332
Spacegroup name	P 1 21 1
Unit cell lengths	104.523, 147.994, 104.563
Unit cell angles	90.00, 94.82, 90.00

Refinement procedure

Resolution	45.860 - 1.790
R-factor	0.1868
Rwork	0.186
R-free	0.22180
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	7svh
RMSD bond length	0.007
RMSD bond angle	0.905
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHASER
Refinement software	PHENIX (1.20_4459)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	45.860	1.854
High resolution limit [Å]	1.790	1.790
Rmerge	0.134	2.275
Rmeas	0.134	2.645
Rpim	0.068	1.331
Number of reflections	296253	29558
<I/σ(I)>	6.43	0.58
Completeness [%]	99.5	97.73
Redundancy	3.7	3.8
CC(1/2)	0.994	0.195

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	0.2 M proline, 0.1M HEPES:NaOH, pH 7.5, 10% (w/v) PEG 3350. Crystals grew in a 2:1 protein:crystallant ratio at a 11.4 mg/mL final protein concentration. Inhibitor was incubated with protein prior to tray setup.