5KA4
Protein Tyrosine Phosphatase 1B T178A mutant, open state
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2015-07-27 |
| Detector | MAR scanner 300 mm plate |
| Wavelength(s) | 1.03 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 117.205, 46.501, 59.911 |
| Unit cell angles | 90.00, 90.39, 90.00 |
Refinement procedure
| Resolution | 35.094 - 2.185 |
| R-factor | 0.2087 |
| Rwork | 0.207 |
| R-free | 0.24220 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.440 |
| Data scaling software | Aimless (0.5.9) |
| 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 | 2.210 |
| High resolution limit [Å] | 2.170 | 5.890 | 2.170 |
| Rmerge | 0.124 | 0.050 | 0.498 |
| Total number of observations | 40632 | ||
| Number of reflections | 15410 | ||
| <I/σ(I)> | 9.7 | ||
| Completeness [%] | 91.3 | 81.8 | 87.5 |
| Redundancy | 2.6 | 2.7 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 277 | 0.1 M Tris, pH 8.0, 0.2 M MgCl2, 17% PEG8000 |
