3QKQ
Protein Tyrosine Phosphatase 1B - W179F mutant bound with vanadate
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2009-01-08 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.5418 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 88.620, 88.620, 104.320 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 38.370 - 2.200 |
R-factor | 0.1987 |
Rwork | 0.196 |
R-free | 0.25380 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2CM2 with the active site water molecules removed |
RMSD bond length | 0.009 |
RMSD bond angle | 1.172 |
Data scaling software | d*TREK (9.4SSI) |
Phasing software | PHASER (2.1.4) |
Refinement software | PHENIX (1.6.4_486) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 38.370 | 38.370 | 2.280 |
High resolution limit [Å] | 2.200 | 4.740 | 2.200 |
Rmerge | 0.108 | 0.049 | 0.494 |
Total number of observations | 13852 | 13210 | |
Number of reflections | 24220 | ||
<I/σ(I)> | 7.9 | 19.4 | 2.7 |
Completeness [%] | 98.7 | 99.2 | 97.3 |
Redundancy | 5.51 | 5.22 | 5.61 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 277 | 2uL of protein solution, 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 protein solution was prepared with 15 uL of 12 mg/mL PTP1B W179F in 10 mM Tris pH 7.5, 25 mM NaCl, 0.2 mM EDTA and 3 mM DTT, and 0.5 uL of 60 mM of sodium vanadate. The well solution was 500 uL of precipitant solution., vapor diffusion, sitting drop, temperature 277K |