5JDI
Trypanosoma brucei PTR1 in complex with cofactor and inhibitor NMT-H024 (compound 2)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I03 |
| Synchrotron site | Diamond |
| Beamline | I03 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-04-29 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.9184 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 74.880, 90.840, 82.900 |
| Unit cell angles | 90.00, 115.70, 90.00 |
Refinement procedure
| Resolution | 57.700 - 1.380 |
| R-factor | 0.1168 |
| Rwork | 0.115 |
| R-free | 0.15046 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2x9g |
| RMSD bond length | 0.027 |
| RMSD bond angle | 2.391 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 57.700 | 1.450 |
| High resolution limit [Å] | 1.380 | 1.380 |
| Rmerge | 0.059 | 0.339 |
| Number of reflections | 204222 | |
| <I/σ(I)> | 9.6 | 2.8 |
| Completeness [%] | 99.7 | 99.4 |
| Redundancy | 3.1 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 298 | Protein solution: 6 g/L in 20 mM Tris-HCl pH 7.5, 10 mM DTT; Crystallization buffer: 0.1 M sodium citrate pH 5, 2.25 M sodium acetate |
