2PA5
Crystal structure of human protein tyrosine phosphatase PTPN9
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-03-03 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.95370 |
| Spacegroup name | P 1 |
| Unit cell lengths | 39.965, 57.427, 66.446 |
| Unit cell angles | 77.44, 78.22, 80.41 |
Refinement procedure
| Resolution | 33.960 - 1.600 |
| R-factor | 0.15726 |
| Rwork | 0.156 |
| R-free | 0.18792 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2hnq |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.434 |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 33.960 | 1.690 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.063 | 0.379 |
| Number of reflections | 71616 | |
| <I/σ(I)> | 9 | 2.1 |
| Completeness [%] | 96.9 | 95.3 |
| Redundancy | 2 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.15 | 293 | 25% PEG 3350, 0.2 M Potassium thiocyanate, 10% Ethylene glycol, 0.1 M Bis-Tris propane pH 6.15, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
