5X8C
AMPPCP and TMP bound crystal structure of thymidylate kinase from thermus thermophilus HB8
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU ULTRAX 18 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2013-07-18 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 1.54179 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 47.100, 47.530, 152.280 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.770 - 2.070 |
| R-factor | 0.18197 |
| Rwork | 0.180 |
| R-free | 0.21903 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5x7j |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.700 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.770 | 2.120 |
| High resolution limit [Å] | 2.070 | 2.070 |
| Number of reflections | 21652 | |
| <I/σ(I)> | 13.5 | |
| Completeness [%] | 99.7 | |
| Redundancy | 7.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 295 | 0.2M MgCl2.6H2O, 0.1 M Tris hydrochloride, 30% PEG 4000 |
