2WOW
Trypanosoma brucei trypanothione reductase with NADP and trypanothione bound
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2009-05-15 |
| Detector | RIGAKU RAXIS IV |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 101.700, 63.700, 169.600 |
| Unit cell angles | 90.00, 97.60, 90.00 |
Refinement procedure
| Resolution | 19.868 - 2.200 |
| R-factor | 0.175 |
| Rwork | 0.172 |
| R-free | 0.22630 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2woi |
| RMSD bond length | 0.023 |
| RMSD bond angle | 1.966 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0088) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.900 | 2.260 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.100 | 0.370 |
| Number of reflections | 109305 | |
| <I/σ(I)> | 15.6 | 3.8 |
| Completeness [%] | 95.4 | 90.5 |
| Redundancy | 3.5 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | 15MG/ML PROTEIN IN 25MM HEPES PH 7.5, 50MM NABR EQUILIBRATED AGAINST 24% MPD, 10% PEG3350, 40MM IMIDAZOLE PH 8.0 |
