5FUW
catalytic domain of Thymidine kinase from Trypanosoma brucei with dTMP or dThd
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I02 |
| Synchrotron site | Diamond |
| Beamline | I02 |
| Temperature [K] | 100 |
| Spacegroup name | P 43 2 2 |
| Unit cell lengths | 114.999, 114.999, 104.770 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 115.000 - 2.200 |
| R-factor | 0.1861 |
| Rwork | 0.185 |
| R-free | 0.20126 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5fuv |
| RMSD bond length | 0.022 |
| RMSD bond angle | 2.160 |
| 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] | 64.240 | 2.270 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.100 | 0.880 |
| Number of reflections | 36299 | |
| <I/σ(I)> | 11.8 | 2.6 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 11.6 | 10.8 |
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 |
