3ZV2
Human protein-tyrosine phosphatase 1b C215A, S216A mutant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | MAR scanner 345 mm plate |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 88.450, 88.450, 103.990 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 40.700 - 2.800 |
| R-factor | 0.21006 |
| Rwork | 0.207 |
| R-free | 0.26772 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2hnq |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.806 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALEPACK |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.870 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.130 | 0.460 |
| Number of reflections | 11735 | |
| <I/σ(I)> | 6.8 | 1.5 |
| Completeness [%] | 97.4 | 97.7 |
| Redundancy | 3.17 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 0.1 M HEPES (PH 7.5), 200 MM MAGNESIUM ACETATE, 12-16% PEG 8K |
