8EWT

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)	1.03
Spacegroup name	P 43 21 2
Unit cell lengths	108.440, 108.440, 161.518
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.220 - 2.030
R-factor	0.1872
Rwork	0.186
R-free	0.22640
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	7svf
RMSD bond length	0.007
RMSD bond angle	0.827
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]	48.220	2.103
High resolution limit [Å]	2.030	2.030
Rmerge	0.213	1.811
Rmeas	0.230	2.044
Rpim	0.084	0.908
Number of reflections	62279	5470
<I/σ(I)>	6.08	0.6
Completeness [%]	96.9	88.3
Redundancy	6.2	4.2
CC(1/2)	0.986	0.146

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	10% (w/v) PEG 4000, 20% (v/v) isopropanol. Protein was incubated with probe and then concentrated to 7.08 mg/mL. Protein crystallized in a 1:2 protein:crystallant ratio.