2WYE
The quorum quenching N-acyl homoserine lactone acylase PvdQ is an Ntn- Hydrolase with an unusual substrate-binding pocket
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-02-02 |
| Detector | ADSC CCD |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 120.080, 163.940, 93.610 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 1.800 |
| R-factor | 0.16141 |
| Rwork | 0.160 |
| R-free | 0.18890 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1keh |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.198 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0096) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.930 | 1.900 |
| High resolution limit [Å] | 1.700 | 1.800 |
| Rmerge | 0.040 | 0.340 |
| Number of reflections | 85309 | |
| <I/σ(I)> | 16.89 | 2.3 |
| Completeness [%] | 99.8 | 99.7 |
| Redundancy | 4.08 | 4.05 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 9 | PROTEIN WAS CRYSTALLIZED FROM 24% PEG 6000, 100 MM BICINE PH 9.1 |
