1E9A
Human thymidylate kinase complexed with the bisubstrate inhibitor AZTP5A
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 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 101.600, 101.600, 49.850 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.500 - 1.600 |
| R-factor | 0.189 * |
| Rwork | 0.189 |
| R-free | 0.22000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.400 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 24.500 | 1.700 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.046 * | 0.361 * |
| Total number of observations | 180754 * | |
| Number of reflections | 34575 | |
| <I/σ(I)> | 16.3 | 3.5 |
| Completeness [%] | 98.9 | 98.6 * |
| Redundancy | 5.2 | 4.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8 | 20 * | Ostermann, N., (2000) Structure (London), 8, 629. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | nucleotide | ||
| 2 | 1 | drop | TMPK | 28 (mg/ml) | |
| 3 | 1 | drop | 50 (mM) | ||
| 4 | 1 | drop | 200 (mM) | ||
| 5 | 1 | drop | Tris-HCl | 50 (mM) | |
| 6 | 1 | reservoir | PEG3350 | 15-22 (%(w/v)) | |
| 7 | 1 | reservoir | dead sea water | 5 (%(v/v)) | |
| 8 | 1 | reservoir | Tris-HCl | 100 (mM) |
