2WOI
Trypanothione reductase from Trypanosoma brucei
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-12-17 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 101.800, 63.620, 169.820 |
| Unit cell angles | 90.00, 97.90, 90.00 |
Refinement procedure
| Resolution | 46.913 - 2.100 |
| R-factor | 0.162 |
| Rwork | 0.160 |
| R-free | 0.20820 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1aog |
| RMSD bond length | 0.024 |
| RMSD bond angle | 1.977 |
| 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] | 46.900 | 2.150 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.120 | 0.430 |
| Number of reflections | 125932 | |
| <I/σ(I)> | 13.8 | 3.1 |
| Completeness [%] | 97.9 | 78.2 |
| Redundancy | 3.7 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 15MG/ML PROTEIN IN 25MM HEPES PH 7.5, 50MM NABR EQUILIBRATED AGAINST 24% MPD, 10% PEG 3350, 40MM IMIDAZOLE PH 8.0 |
