2OB3
Structure of Phosphotriesterase mutant H257Y/L303T
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-08-10 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | P 1 |
Unit cell lengths | 43.362, 45.374, 79.211 |
Unit cell angles | 104.86, 93.27, 97.81 |
Refinement procedure
Resolution | 30.000 - 1.040 |
R-factor | 0.105 |
Rwork | 0.105 |
R-free | 0.12700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1p6b |
RMSD bond length | 0.015 |
RMSD bond angle | 0.029 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | SHELX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.080 |
High resolution limit [Å] | 1.040 | 1.040 |
Rmerge | 0.061 | 0.188 |
Number of reflections | 235873 | |
<I/σ(I)> | 15.6 | 6.3 |
Completeness [%] | 85.5 | 41.4 |
Redundancy | 3.4 | 2.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 0.1M bis tris, pH 6.5, 12% PEG MME 5000, VAPOR DIFFUSION, HANGING DROP, temperature 293K |