8ESL
Bile Salt Hydrolase from a Bacteroidales species with covalent inhibitor bound
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-02-27 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.00 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 63.142, 66.812, 321.831 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.070 - 3.110 |
R-factor | 0.2769 |
Rwork | 0.277 |
R-free | 0.30510 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | AlphaFold2 model of the protein |
RMSD bond length | 0.002 |
RMSD bond angle | 0.410 |
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] | 45.070 | 3.221 |
High resolution limit [Å] | 3.110 | 3.110 |
Rmerge | 0.240 | 1.710 |
Rmeas | 0.287 | 2.057 |
Rpim | 0.155 | 1.115 |
Number of reflections | 24835 | 2378 |
<I/σ(I)> | 3.81 | 0.74 |
Completeness [%] | 94.8 | 80.39 |
Redundancy | 3.4 | 3.3 |
CC(1/2) | 0.978 | 0.121 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.1 M HEPES: NaOH, pH 7.5, 25% (w/v) PEG 1000. 50 mL protein at 2.5 uM was incubated with 50 uM inhibitor for 1h at 37oC. Mixture was washed 3x with buffer in a spin concentrator and then concentrated to 6.77 mg/mL final concentration. Crystals formed in conditions with 1:2 ratio of protein:mother liquor. |