4H1I
Structure of human thymidylate synthase at low salt conditions
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 173 |
| Detector technology | IMAGE PLATE |
| Collection date | 2011-05-08 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 157.855, 94.927, 131.439 |
| Unit cell angles | 90.00, 122.75, 90.00 |
Refinement procedure
| Resolution | 19.888 - 3.095 |
| R-factor | 0.2344 |
| Rwork | 0.232 |
| R-free | 0.28490 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1hw4 |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.770 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.7.3_928)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.900 | 3.200 |
| High resolution limit [Å] | 3.100 | 3.100 |
| Number of reflections | 29732 | |
| <I/σ(I)> | 8.6 | 2.05 |
| Completeness [%] | 99.6 | 98.6 |
| Redundancy | 6.2 | 5.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | Protein at 5mg/ml, 30% PEG 1500, 15mM ammonium sulfate, 20mM 2-mercaptoethanol, 3% w/v 1,5-Diaminopentane dihydrochloride, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
