2VC7
Structural basis for natural lactonase and promiscuous phosphotriesterase activities
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 86.383, 104.124, 153.051 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 61.660 - 2.050 |
| R-factor | 0.239 |
| Rwork | 0.237 |
| R-free | 0.28700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2vc5 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.119 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 61.660 | 2.150 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.130 | |
| Number of reflections | 141906 | |
| <I/σ(I)> | 13.66 | |
| Completeness [%] | 99.9 | 92.8 |
| Redundancy | 7.25 | 7.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | TRIS-HCL 50MM PH 8, 15-18% W/V PEG 8000 |
