8ETK

Bile salt hydrolase A from Lactobacillus gasseri bound to covalent probe

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 43 21 2
Unit cell lengths	108.538, 108.538, 160.341
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.540 - 1.830
R-factor	0.2004
Rwork	0.200
R-free	0.22470
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	7svf
RMSD bond length	0.007
RMSD bond angle	0.898
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHASER
Refinement software	PHENIX (1.20.1_4487)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.540	1.895
High resolution limit [Å]	1.830	1.830
Rmerge	0.176	4.355
Rmeas	0.183	4.510
Rpim	0.048	1.166
Number of reflections	84823	8358
<I/σ(I)>	12.09	0.86
Completeness [%]	99.9	99.9
Redundancy	14.5	14.9
CC(1/2)	0.998	0.357

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	0.1 M sodium phosphate dibasic:citric acid, pH 4.2, 40% (v/v) PEG 300. Probe was incubated with protein before tray setup at 6.94 mg/mL protein concentration. Crystals formed in a 1:1 protein:crystallant ratio.