5FUV
catalytic domain of Thymidine kinase from Trypanosoma brucei with dThd
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I04 |
| Synchrotron site | Diamond |
| Beamline | I04 |
| Temperature [K] | 100 |
| Spacegroup name | P 43 2 2 |
| Unit cell lengths | 114.680, 114.680, 105.600 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 114.680 - 2.300 |
| R-factor | 0.18016 |
| Rwork | 0.179 |
| R-free | 0.20745 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1w4r |
| RMSD bond length | 0.023 |
| RMSD bond angle | 2.217 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 44.250 | 2.390 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.080 | 1.020 |
| Number of reflections | 31864 | |
| <I/σ(I)> | 17 | 2.6 |
| Completeness [%] | 99.9 | 99.9 |
| Redundancy | 14.3 | 14.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 0.1 M HEPES PH 7.0, 0.8 M SUCCINIC ACID 1 MM TMP, 1 MM APPNHP, 3 MM MGCL2 |
