5KAA
Protein Tyrosine Phosphatase 1B Delta helix 7, P185G mutant, open state
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E+ SUPERBRIGHT |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-07-22 |
Detector | RIGAKU SATURN 944+ |
Wavelength(s) | 1.54 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 88.330, 88.330, 72.373 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 38.248 - 1.968 |
R-factor | 0.1747 |
Rwork | 0.173 |
R-free | 0.21040 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5ka0 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.055 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER (2.5.6) |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.000 |
High resolution limit [Å] | 1.968 | 5.350 | 1.970 |
Rmerge | 0.055 | 0.029 | 0.221 |
Total number of observations | 235875 | ||
Number of reflections | 23338 | ||
<I/σ(I)> | 11.8 | ||
Completeness [%] | 99.3 | 99.8 | 92.6 |
Redundancy | 10.1 | 10.3 | 5.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 277 | 0.1 M HEPES, pH 8.0, 0.2 M MgCl2, 19% PEG8000 |