1NN0
Crystal structure of human thymidylate kinase with ddTMP and ADP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID2 |
Synchrotron site | ESRF |
Beamline | ID2 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Wavelength(s) | 0.9887 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 100.535, 100.535, 49.963 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 70.700 * - 1.600 |
Rwork | 0.211 |
R-free | 0.26500 |
Structure solution method | FOURIER SYNTHESIS |
RMSD bond length | 0.014 * |
RMSD bond angle | 1.700 * |
Data reduction software | XDS |
Data scaling software | XDS |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 70.700 | 1.600 |
High resolution limit [Å] | 1.550 | 1.550 |
Rmerge | 0.073 | 0.364 * |
Total number of observations | 119378 * | |
Number of reflections | 35723 | |
<I/σ(I)> | 7.24 | 1.32 |
Completeness [%] | 94.7 * | 96.4 |
Redundancy | 3.3 | 2.6 |
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 | ADP | 2 (mM) |