6PXA
The crystal structure of chloramphenicol acetyltransferase-like protein from Vibrio fischeri ES114 in complex with taurocholic acid
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-03-19 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.9789 |
| Spacegroup name | P 1 |
| Unit cell lengths | 43.519, 121.363, 146.170 |
| Unit cell angles | 89.40, 89.91, 87.60 |
Refinement procedure
| Resolution | 46.900 - 1.820 |
| R-factor | 0.1993 |
| Rwork | 0.197 |
| R-free | 0.23770 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5ux9 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.006 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | PHENIX (1.15.2_3472) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.900 | 1.840 |
| High resolution limit [Å] | 1.820 | 1.820 |
| Rmerge | 0.084 | 0.718 |
| Rmeas | 0.100 | 0.850 |
| Rpim | 0.053 | 0.447 |
| Number of reflections | 257772 | 9761 |
| <I/σ(I)> | 25.3 | 1.4 |
| Completeness [%] | 96.3 | 92 |
| Redundancy | 3.4 | 3.2 |
| CC(1/2) | 0.987 | 0.783 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 289 | 0.2 M Sodium acetate, 0.1 M Tris, 16% (w/v) PEG4000 |
