3PR8
Structure of Glutathione S-transferase(PP0183) from Pseudomonas putida in complex with GSH
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 | 2010-04-22 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9793 |
| Spacegroup name | P 1 |
| Unit cell lengths | 48.032, 66.012, 88.853 |
| Unit cell angles | 89.92, 85.55, 86.50 |
Refinement procedure
| Resolution | 40.000 - 1.800 |
| R-factor | 0.1727 |
| Rwork | 0.171 |
| R-free | 0.20250 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3lxz |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.405 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 40.000 | 40.000 | 1.830 |
| High resolution limit [Å] | 1.800 | 4.880 | 1.800 |
| Rmerge | 0.080 | 0.064 | 0.376 |
| Number of reflections | 97182 | ||
| <I/σ(I)> | 10.7 | ||
| Completeness [%] | 96.8 | 94.4 | 95.8 |
| Redundancy | 2.2 | 2.2 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 298 | 0.1M Bis-Tris pH5.5, 1% PEG 3350, 1.0M Ammonium Sulfate, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
