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 |