1E9C
Mutant human thymidylate kinase complexed with TMP and APPNP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Temperature [K] | 100 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 101.300, 101.300, 49.200 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 70.000 - 1.600 |
| R-factor | 0.209 * |
| Rwork | 0.209 |
| R-free | 0.26800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.800 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 70.000 | 1.700 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.077 * | 0.330 * |
| Total number of observations | 165640 * | |
| Number of reflections | 31952 * | |
| <I/σ(I)> | 17.7 | 2.9 |
| Completeness [%] | 93.0 | 82.7 |
| Redundancy | 5.2 | 3.1 |
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) |
