5KAC
Protein Tyrosine Phosphatase 1B 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 | 2015-09-15 |
| Detector | RIGAKU SATURN 944+ |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 88.375, 88.375, 72.342 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 38.267 - 1.900 |
| R-factor | 0.1703 |
| Rwork | 0.168 |
| R-free | 0.21090 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5k9v |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.608 |
| 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 | 1.930 |
| High resolution limit [Å] | 1.900 | 5.160 | 1.900 |
| Rmerge | 0.036 | 0.027 | 0.158 |
| Total number of observations | 246127 | ||
| Number of reflections | 22800 | ||
| <I/σ(I)> | 19.4 | ||
| Completeness [%] | 87.3 | 98.7 | 40.7 |
| Redundancy | 10.8 | 10.4 | 8.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 277 | 0.1 M Tris, pH 7.4, 0.2 M MgCl2, 18% PEG8000 |
