6BU7
Crystal structure of Trypanothione Reductase from Trypanosoma brucei in complex with inhibitor RD130 1-[2-(Piperidin-4-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 | 117.283, 117.283, 224.535 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.500 - 2.730 |
R-factor | 0.1983 |
Rwork | 0.196 |
R-free | 0.24150 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2woi |
RMSD bond length | 0.004 |
RMSD bond angle | 0.618 |
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] | 46.500 | 2.820 |
High resolution limit [Å] | 2.730 | 2.730 |
Rmerge | 0.104 | 1.469 |
Rmeas | 0.111 | 1.583 |
Rpim | 0.037 | 0.569 |
Number of reflections | 42552 | 4132 |
<I/σ(I)> | 12.6 | 1.04 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 8.8 | 7.3 |
CC(1/2) | 0.999 | 0.587 |
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). |