2G59
Crystal Structure of the Catalytic Domain of Protein Tyrosine Phosphatase from Homo sapiens
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X12C |
| Synchrotron site | NSLS |
| Beamline | X12C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-02-17 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1.1 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 73.869, 59.723, 76.995 |
| Unit cell angles | 90.00, 102.31, 90.00 |
Refinement procedure
| Resolution | 31.830 - 2.190 |
| R-factor | 0.199 |
| Rwork | 0.199 |
| R-free | 0.23700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ahs |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.300 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.270 |
| High resolution limit [Å] | 2.190 | 2.190 |
| Number of reflections | 33737 | |
| <I/σ(I)> | 11.5 | |
| Completeness [%] | 97.7 | 90.8 |
| Redundancy | 3.2 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 298 | 0.1 M Bis-Tris, 2.0 M Sodium Chloride, 5% PEG 3350, 5 mM Calcium Chloride, 10 mM Sodium Phosphate, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
