2CCG
Crystal structure of His-tagged S. aureus thymidylate kinase complexed with thymidine monophosphate (TMP)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-11-12 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 54.540, 51.270, 72.940 |
| Unit cell angles | 90.00, 103.63, 90.00 |
Refinement procedure
| Resolution | 29.160 - 2.300 |
| R-factor | 0.2 |
| Rwork | 0.200 |
| R-free | 0.24600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB ENTRIES 4TMK AND 1GSI |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.300 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.380 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.040 | 0.250 |
| Number of reflections | 15887 | |
| <I/σ(I)> | 25.1 | 4.6 |
| Completeness [%] | 89.2 | 49 |
| Redundancy | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.6 | 1M LICL, 0.1M NA CACODYLATE PH6.6, 18% PEG 6000, pH 6.60 |
