2WOV
Trypanosoma brucei trypanothione reductase with bound NADP.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2009-01-13 |
Detector | RIGAKU RAXIS IV |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 100.870, 63.450, 169.350 |
Unit cell angles | 90.00, 97.85, 90.00 |
Refinement procedure
Resolution | 19.847 - 2.500 |
R-factor | 0.182 |
Rwork | 0.179 |
R-free | 0.25080 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2woi |
RMSD bond length | 0.017 |
RMSD bond angle | 1.730 |
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 | 2.560 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.110 | 0.400 |
Number of reflections | 72546 | |
<I/σ(I)> | 14.8 | 3.6 |
Completeness [%] | 93.3 | 85.6 |
Redundancy | 3.6 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 15MG/ML PROTEIN IN 25MM HEPES PH 7.5 AND 50MM NABR EQUILIBRATED AGAINST 24% MPD, 10% PEG3350 AND 40MM IMIDAZOLE PH 8.0. |