8ETE

Bile Salt Hydrolase from B. longum 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 32 2 1
Unit cell lengths	100.085, 100.085, 165.187
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	47.890 - 2.300
R-factor	0.2531
Rwork	0.251
R-free	0.28380
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2hf0
RMSD bond length	0.003
RMSD bond angle	0.549
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]	47.890	2.382
High resolution limit [Å]	2.300	2.300
Rmerge	0.325
Rmeas	0.342
Rpim	0.105
Number of reflections	43164	4255
<I/σ(I)>	7.05
Completeness [%]	97.8	83.71
Redundancy	10.4	10.2
CC(1/2)	0.996	0.122

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	0.1 M sodium acetate, 0.1 M HEPES:NaOH pH 7.5, 25% (w/v) PEG4000, 0.2 M lithium sulfate. Protein crystallized in a 1:2 protein:crystallant ratio. Protein was incubated with inhibitor prior to tray setup and was 8.55 mg/mL final concentration.