7S4F
Protein Tyrosine Phosphatase 1B - F182Q mutant bound with Hepes
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2007-06-20 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.55 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 88.316, 88.316, 103.895 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 22.887 - 1.650 |
R-factor | 0.181 |
Rwork | 0.180 |
R-free | 0.20310 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3i80 |
RMSD bond length | 0.006 |
RMSD bond angle | 1.034 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.6.4_486) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.710 |
High resolution limit [Å] | 1.650 | 3.550 | 1.650 |
Rmerge | 0.048 | 0.033 | 0.491 |
Number of reflections | 53917 | 5717 | 3773 |
<I/σ(I)> | 24.6 | ||
Completeness [%] | 94.8 | 96 | 67.3 |
Redundancy | 5.2 | 5.8 | 3 |
CC(1/2) | 0.701 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 277 | 2uL of protein solution (12 mg/mL PTP1B F182Q in 10 mM Tris pH 7.5, 25 mM NaCl, 0.2 mM EDTA and 3 mM DTT), 0.5 uL sucrose 30% (w/v) and 3 uL of precipitant solution (0.1 M Hepes pH 7.5, 0.2 M magnesium acetate and 15-20% polyethylene glycol 8000). The well solution was 500 uL of precipitant solution. |