5KA8
Protein Tyrosine Phosphatase 1B L192A mutant, 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 | 2014-12-02 |
| Detector | RIGAKU SATURN 944+ |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 88.896, 88.896, 105.840 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 36.175 - 1.971 |
| R-factor | 0.1904 |
| Rwork | 0.188 |
| R-free | 0.23160 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1sug |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.395 |
| 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 | 2.000 |
| High resolution limit [Å] | 1.970 | 5.350 | 1.970 |
| Rmerge | 0.060 | 0.033 | 0.453 |
| Total number of observations | 695556 | ||
| Number of reflections | 34376 | ||
| <I/σ(I)> | 11.7 | ||
| Completeness [%] | 99.1 | 99.7 | 89.7 |
| Redundancy | 20.2 | 20.4 | 11.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 277 | 0.1 M HEPES, pH 8.0, 0.2 M MgCl2, 19% PEG8000 |
