3JQA
Crystal structure of pteridine reductase 1 (PTR1) from Trypanosoma brucei in ternary complex with cofactor (NADP+) and inhibitor 2-amino-1,9-dihydro-6H-purine-6-thione (DX4)
Replaces: 3BMGExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-05-21 |
| Detector | MARMOSAIC 325 mm CCD |
| Wavelength(s) | 0.87300 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 74.997, 90.834, 82.640 |
| Unit cell angles | 90.00, 115.50, 90.00 |
Refinement procedure
| Resolution | 57.640 - 1.900 |
| R-factor | 0.149 |
| Rwork | 0.147 |
| R-free | 0.18900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2c7v |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.342 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.2.17) |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 57.640 | 57.640 | 2.000 |
| High resolution limit [Å] | 1.900 | 6.010 | 1.900 |
| Rmerge | 0.057 | 0.028 | 0.320 |
| Total number of observations | 7169 | 37751 | |
| Number of reflections | 78741 | ||
| <I/σ(I)> | 9.9 | 7 | 2.1 |
| Completeness [%] | 99.9 | 98.3 | 99.9 |
| Redundancy | 3 | 2.8 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 293 | 2-3M Sodium acetate, 10-100mM Sodium citrate, pH 4.0-6.0, VAPOR DIFFUSION, temperature 293K |
