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 |