3PS5
Crystal structure of the full-length Human Protein Tyrosine Phosphatase SHP-1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CAMD BEAMLINE GCPCC |
| Synchrotron site | CAMD |
| Beamline | GCPCC |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-12-01 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1.3807 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 231.919, 231.919, 78.852 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 115.960 - 3.100 |
| R-factor | 0.2272 |
| Rwork | 0.225 |
| R-free | 0.27576 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2b3o |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.855 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 116.000 | 3.210 |
| High resolution limit [Å] | 3.100 | 3.100 |
| Rmerge | 0.086 | 0.596 |
| Number of reflections | 14036 | |
| <I/σ(I)> | 18.1 | 1.5 |
| Completeness [%] | 99.9 | 98.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 278 | 2.5 ul of SHP-1 at 3.5 mg/ml in 25mM Tris-HCl, beta-mercaptoethanol, 1mM EDTA mixed with 2.5 ul of 1.8M ammonium sulfate, 0.1M glycine, 0.1M Tris-HCl, with the addition of 0.5 ul 14mM deoxy Big Chap to form the final drop., pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 278K |
