5KA7
Protein Tyrosine Phosphatase 1B T178A mutant in complex with TCS401, closed state
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E+ SUPERBRIGHT |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-07-20 |
| Detector | RIGAKU SATURN 944+ |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 88.564, 88.564, 104.110 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 44.282 - 2.061 |
| R-factor | 0.1849 |
| Rwork | 0.183 |
| R-free | 0.21370 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1c88 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.083 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER (2.5.6) |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.100 |
| High resolution limit [Å] | 2.060 | 5.590 | 2.060 |
| Rmerge | 0.072 | 0.032 | 0.390 |
| Total number of observations | 315712 | ||
| Number of reflections | 29148 | ||
| <I/σ(I)> | 9.6 | ||
| Completeness [%] | 98.2 | 99.3 | 94.6 |
| Redundancy | 10.8 | 10.2 | 8.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.6 | 277 | 0.1 M Tris, pH 7.6, 0.2 M MgCl2, 24% PEG8000 |
