2OQL
Structure of Phosphotriesterase mutant H254Q/H257F
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2007-01-30 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 |
| Unit cell lengths | 43.528, 45.367, 79.113 |
| Unit cell angles | 104.75, 93.13, 97.97 |
Refinement procedure
| Resolution | 50.000 - 1.800 |
| R-factor | 0.148 |
| Rwork | 0.146 |
| R-free | 0.18900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.417 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.006 | 0.031 |
| Number of reflections | 49147 | |
| <I/σ(I)> | 12.93 | 3.04 |
| Completeness [%] | 91.8 | 70.2 |
| Redundancy | 1.9 | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 0.1M Bis-Tris pH 6.5, 20% PEG MME 5000, Vapor diffusion, sitting drop, temperature 293K |
