2CM3
Structure of Protein Tyrosine Phosphatase 1B (C2)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 |
| Temperature [K] | 93 |
| Detector technology | IMAGE PLATE |
| Detector | RIGAKU RAXIS IV |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 106.850, 95.500, 70.750 |
| Unit cell angles | 90.00, 109.66, 90.00 |
Refinement procedure
| Resolution | 7.000 - 2.100 |
| Rwork | 0.233 |
| R-free | 0.29500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1eeo |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.424 |
| Data reduction software | CrystalClear |
| Data scaling software | CrystalClear |
| Phasing software | CNX |
| Refinement software | CNX (2002) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 27.000 | 2.180 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.060 | 0.140 |
| Number of reflections | 38991 | |
| <I/σ(I)> | 14.8 | 5.6 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 3.7 | 3.75 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 12-16% PEG 3000, 100 MM HEPES PH 7.0-8.0, 200 MM MAGNESIUM ACETATE, 2 MM TCEP |
