5KA3
Protein Tyrosine Phosphatase 1B YAYA (Y152A, Y153A) 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 | 2014-12-02 |
| Detector | RIGAKU SATURN 944+ |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 88.571, 88.571, 104.154 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 44.286 - 2.141 |
| R-factor | 0.2022 |
| Rwork | 0.201 |
| R-free | 0.23670 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1c88 |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.618 |
| 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 | 2.180 |
| High resolution limit [Å] | 2.140 | 5.810 | 2.140 |
| Rmerge | 0.133 | 0.058 | 0.894 |
| Total number of observations | 571351 | ||
| Number of reflections | 26577 | ||
| <I/σ(I)> | 5.5 | ||
| Completeness [%] | 100.0 | 99.8 | 100 |
| Redundancy | 21.5 | 20.2 | 18 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 277 | 0.1 HEPES, pH 7.8, 0.2 M MgCl2, 20.5% PEG8000 |
