8ESI
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] | 293 |
Detector technology | PIXEL |
Collection date | 2021-10-08 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 1.00 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 93.072, 166.801, 103.077 |
Unit cell angles | 90.00, 116.60, 90.00 |
Refinement procedure
Resolution | 49.100 - 2.350 |
R-factor | 0.2103 |
Rwork | 0.210 |
R-free | 0.24360 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2hf0 |
RMSD bond length | 0.002 |
RMSD bond angle | 0.500 |
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] | 49.100 | 2.430 |
High resolution limit [Å] | 2.350 | 2.350 |
Rmerge | 0.177 | 1.889 |
Rmeas | 0.208 | 2.199 |
Rpim | 0.108 | 1.112 |
Number of reflections | 116293 | 11592 |
<I/σ(I)> | 5.4 | 0.88 |
Completeness [%] | 99.6 | 99.6 |
Redundancy | 3.8 | 3.9 |
CC(1/2) | 0.986 | 0.341 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.2 M MgCl2, 0.1 M Tris:HCl pH 8.5, 16% (w/v) PEG 4000. Crystals formed in 1:2 ratio of protein (11.8 mg/mL) to mother liquor. 2.5 uM protein was incubated with 50 uM inhibitor for 1h at 37oC. Mixture was washed 3x with buffer in a spin concentrator and then concentrated to 11.8 mg/mL final concentration. |