1GFY
RESIDUE 259 IS A KEY DETERMINANT OF SUBSTRATE SPECIFICITY OF PROTEIN-TYROSINE PHOSPHATASE 1B AND ALPHA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I711 |
| Synchrotron site | MAX II |
| Beamline | I711 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 88.195, 88.195, 103.728 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 6.000 - 2.130 |
| R-factor | 0.191 |
| Rwork | 0.191 |
| R-free | 0.25000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.019 |
| RMSD bond angle | 3.720 * |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.170 |
| High resolution limit [Å] | 2.130 | 2.130 |
| Rmerge | 0.073 | 0.387 |
| Number of reflections | 26558 | |
| <I/σ(I)> | 14.7 | 3.1 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 5.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 7.5 | pH 7.5 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 100 (mM) | |
| 3 | 1 | drop | EDTA | 0.2 (mM) | |
| 4 | 1 | drop | dithiothreitol | 3 (mM) | |
| 5 | 1 | reservoir | HEPES | 0.1 (M) | |
| 6 | 1 | reservoir | sodium acetate | 0.3-0.4 (M) | or magnesium acetate |
| 7 | 1 | reservoir | PEG8000 | 12-16 (%) |
