3N5E
Crystal Structure of human thymidylate synthase bound to a peptide inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-02-17 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.947 |
| Spacegroup name | P 31 |
| Unit cell lengths | 96.109, 96.109, 82.240 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 83.230 - 2.260 |
| R-factor | 0.18939 |
| Rwork | 0.188 |
| R-free | 0.22136 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ypv |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.496 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 83.330 | 2.380 |
| High resolution limit [Å] | 2.260 | 2.260 |
| Rmerge | 0.071 | 0.303 |
| Number of reflections | 39745 | |
| <I/σ(I)> | 25.9 | 6.7 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 11 | 11.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.3 | 293 | 25% saturated Ammonium Sulfate, 20mM BME, 0.1M TRIS pH8.3, VAPOR DIFFUSION, SITTING DROP, temperature 293.0K |
