2WP5
Trypanosoma brucei trypanothione reductase in complex with 3,4- dihydroquinazoline inhibitor (DDD00065414)
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 | 2007-12-16 |
Detector | ADSC CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 100.940, 63.300, 169.410 |
Unit cell angles | 90.00, 98.09, 90.00 |
Refinement procedure
Resolution | 46.711 - 2.800 |
R-factor | 0.167 |
Rwork | 0.164 |
R-free | 0.21930 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2woi |
RMSD bond length | 0.017 |
RMSD bond angle | 1.795 |
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] | 46.700 | 2.870 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.130 | 0.330 |
Number of reflections | 44043 | |
<I/σ(I)> | 10.8 | 4.37 |
Completeness [%] | 80.5 | 79.9 |
Redundancy | 2.5 | 2.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8 | 15MG/ML PROTEIN IN 25MM HEPES PH 7.5 AND 50MM NABR EQUILIBRATED AGAINST 24% MPD, 10% PEG3350 AND 40MM IMIDAZOLE PH 8.0 |