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 |