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 |