5KAD
Protein Tyrosine Phosphatase 1B N193A 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 | 2015-05-19 |
| Detector | RIGAKU SATURN 944+ |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 47.626, 73.732, 88.123 |
| Unit cell angles | 90.00, 104.40, 90.00 |
Refinement procedure
| Resolution | 28.799 - 1.900 |
| R-factor | 0.1774 |
| Rwork | 0.176 |
| R-free | 0.20490 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1c88 |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.906 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER (2.5.6) |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 28.799 | 50.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 5.160 | 1.900 |
| Rmerge | 0.091 | 0.050 | 0.266 |
| Total number of observations | 145593 | ||
| Number of reflections | 41762 | ||
| <I/σ(I)> | 7.9 | ||
| Completeness [%] | 89.1 | 99.1 | 44.7 |
| Redundancy | 3.5 | 3.6 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 277 | 0.1 M Tris, pH 8.0, 0.2 M MgCl2, 17.5% PEG8000 |
