4O1U
Crystal structure of human thymidylate synthase mutant Y202C
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-12-05 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.936 |
| Spacegroup name | P 31 |
| Unit cell lengths | 96.230, 96.230, 83.770 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 48.120 - 2.260 |
| R-factor | 0.17343 |
| Rwork | 0.172 |
| R-free | 0.21006 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3n5g |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.435 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.120 | 2.380 |
| High resolution limit [Å] | 2.260 | 2.260 |
| Rmerge | 0.067 | 0.378 |
| Number of reflections | 39688 | |
| <I/σ(I)> | 12 | 3.7 |
| Completeness [%] | 97.6 | 98.6 |
| Redundancy | 3.8 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.3 | 300 | 35% saturated Ammonium Sulfate + 20mM BME + 0.1M TRIS, pH 8.3, VAPOR DIFFUSION, HANGING DROP, temperature 300K |
