5L42
Leishmania major Pteridine reductase 1 (PTR1) in complex with compound 3
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ELETTRA BEAMLINE 5.2R |
| Synchrotron site | ELETTRA |
| Beamline | 5.2R |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-08-05 |
| Detector | DECTRIS PILATUS 2M |
| Wavelength(s) | 0.999 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 94.699, 104.190, 137.042 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.350 - 2.100 |
| R-factor | 0.16719 |
| Rwork | 0.165 |
| R-free | 0.21383 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2bfa |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.955 |
| 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] | 47.350 | 2.210 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.134 | 0.289 |
| Number of reflections | 79156 | |
| <I/σ(I)> | 5.6 | 2.9 |
| Completeness [%] | 99.5 | 99.5 |
| Redundancy | 4.2 | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | Protein solution: 12.5 mg/mL in 20 mM Sodium Acetate pH 5.3 and 10 mM DTT; Crystallisation buffer: 12% PEG4600, 100 mM Sodium Acetate pH 5.5 and 120-160 mM Calcium Acetate |
