2CM2
Structure of Protein Tyrosine Phosphatase 1B (P212121)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 |
Temperature [K] | 277 |
Detector technology | IMAGE PLATE |
Detector | RIGAKU RAXIS-IV |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 40.640, 69.210, 100.770 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 1.500 |
Rwork | 0.198 |
R-free | 0.23350 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1eeo |
RMSD bond length | 0.011 |
RMSD bond angle | 1.538 |
Data reduction software | CrystalClear |
Data scaling software | CrystalClear |
Phasing software | CNX |
Refinement software | CNX (2000) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 10.000 | 1.550 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.050 | 0.320 |
Number of reflections | 44327 | |
<I/σ(I)> | 16 | 3 |
Completeness [%] | 96.0 | 73 |
Redundancy | 4 | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5.9 | 100 MM SODIUM/POTASSIUM PHOSPHATE PH 5.9 AND 25%-35% METHYLPENTANEDIOL |