5KAA
Protein Tyrosine Phosphatase 1B Delta helix 7, P185G 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 | 2015-07-22 |
| Detector | RIGAKU SATURN 944+ |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 88.330, 88.330, 72.373 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 38.248 - 1.968 |
| R-factor | 0.1747 |
| Rwork | 0.173 |
| R-free | 0.21040 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5ka0 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.055 |
| Data reduction software | HKL-2000 |
| 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] | 1.968 | 5.350 | 1.970 |
| Rmerge | 0.055 | 0.029 | 0.221 |
| Total number of observations | 235875 | ||
| Number of reflections | 23338 | ||
| <I/σ(I)> | 11.8 | ||
| Completeness [%] | 99.3 | 99.8 | 92.6 |
| Redundancy | 10.1 | 10.3 | 5.4 |
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 |
