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. |