5KA9
Protein Tyrosine Phosphatase 1B L192A mutant in complex with TCS401, open 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 | 2015-06-18 |
| Detector | RIGAKU SATURN 944+ |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 88.709, 88.709, 106.218 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 44.355 - 2.070 |
| R-factor | 0.1907 |
| Rwork | 0.189 |
| R-free | 0.23020 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5ka8 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.841 |
| 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 | 2.110 |
| High resolution limit [Å] | 2.070 | 5.620 | 2.070 |
| Rmerge | 0.138 | 0.056 | 0.554 |
| Total number of observations | 318251 | ||
| Number of reflections | 29326 | ||
| <I/σ(I)> | 5 | ||
| Completeness [%] | 97.8 | 99.4 | 93.8 |
| Redundancy | 10.9 | 10.2 | 8.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.8 | 277 | 0.1 M Tris, 0.2 M mgCl2, 18.5% PEG8000 |
