4MQB
Crystal structure of thymidylate kinase from Staphylococcus aureus in complex with 2-(N-morpholino)ethanesulfonic acid
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-07-25 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97856 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 46.134, 90.457, 49.524 |
| Unit cell angles | 90.00, 101.64, 90.00 |
Refinement procedure
| Resolution | 25.620 - 1.550 |
| R-factor | 0.14528 |
| Rwork | 0.142 |
| R-free | 0.19845 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4f4i |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.926 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.580 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.060 | 0.520 |
| Number of reflections | 57729 | |
| <I/σ(I)> | 20.1 | 2.9 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 3.7 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 293 | 0.2 M MgCl2, 0.1 M MMES buffer, 20% PEG6000, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
