2VC5
Structural basis for natural lactonase and promiscuous phosphotriesterase activities
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-06-17 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 87.160, 104.820, 155.360 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 44.900 - 2.600 |
| R-factor | 0.225 |
| Rwork | 0.222 |
| R-free | 0.28200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1dpm |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.061 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 44.900 |
| High resolution limit [Å] | 2.590 |
| Rmerge | 0.160 |
| Number of reflections | 85611 |
| <I/σ(I)> | 11.69 |
| Completeness [%] | 95.3 |
| Redundancy | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | 50MM TRIS-HCL PH 8, 15-18% PEG 8000, 0.1MM COCL2 |
