7KEN
Protein Tyrosine Phosphatase 1B, D289A mutant, apo state
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.1 |
| Synchrotron site | ALS |
| Beamline | 5.0.1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-07-24 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.97741 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 88.314, 88.314, 104.155 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 76.480 - 1.800 |
| R-factor | 0.20561 |
| Rwork | 0.204 |
| R-free | 0.24369 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6b90 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.418 |
| Data reduction software | xia2 |
| Data scaling software | xia2 |
| Phasing software | PHENIX |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 76.480 | 1.830 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.178 | |
| Rmeas | 0.187 | |
| Rpim | 0.056 | |
| Number of reflections | 40989 | 2129 |
| <I/σ(I)> | 6.2 | 0.3 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 10.8 | |
| CC(1/2) | 0.997 | 0.315 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | 100 mM HEPES, 200 mM magnesium acetate, 14% PEG8000 |
