1NN5
Crystal structure of human thymidylate kinase with d4TMP + AppNHp
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X11 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Wavelength(s) | 0.9076 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 101.100, 101.100, 49.800 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 35.500 - 1.500 |
Rwork | 0.192 |
R-free | 0.21500 |
Structure solution method | FOURIER SYNTHESIS |
RMSD bond length | 0.009 * |
RMSD bond angle | 1.600 * |
Data reduction software | XDS |
Data scaling software | XDS |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.500 | 1.600 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.050 | 0.311 * |
Total number of observations | 182998 * | |
Number of reflections | 41213 | |
<I/σ(I)> | 15.11 | 3.65 |
Completeness [%] | 98.4 | 99.8 |
Redundancy | 4.4 | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 15-20% PEG 3350, 100 mM Tris/HCl, pH 8.0, 5% filtered dead sea water, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 2 (mM) | |
2 | 1 | drop | AppNHp | 2 (mM) |