6BTL
Crystal structure of Trypanothione Reductase from Trypanosoma brucei in complex with inhibitor RD117 1-[2-(Piperazin-1-yl)ethyl]-5-{5-[1-(pyrrolidin-1-yl)cyclohexyl]-1,3-thiazol-2-yl}-1H-indole
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Temperature [K] | 93 |
Detector technology | PIXEL |
Collection date | 2016-12-03 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 1.0332 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 117.664, 117.664, 225.163 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.671 - 2.797 |
R-factor | 0.1985 |
Rwork | 0.197 |
R-free | 0.23630 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2woi |
RMSD bond length | 0.004 |
RMSD bond angle | 0.985 |
Data reduction software | XDS |
Data scaling software | autoPROC |
Phasing software | PHASER |
Refinement software | PHENIX ((1.12_2829: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.700 | 2.900 |
High resolution limit [Å] | 2.797 | 2.797 |
Rmerge | 0.137 | 1.609 |
Rmeas | 0.146 | 1.728 |
Rpim | 0.049 | 0.618 |
Number of reflections | 39719 | 3684 |
<I/σ(I)> | 16.8 | |
Completeness [%] | 99.4 | 95 |
Redundancy | 8.6 | 7.2 |
CC(1/2) | 0.998 | 0.423 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 294 | Adding 5 microL of 10 mM inhibitor in DMSO to 95 microL of protein solution (10mg/ml; 20 mM TRIS, pH8.0), then mixing 2 microL of protein solution with 2 microL of well solution (0.1 M HEPES, pH 7.5, 2.0 M (NH4)2SO4). |