4EGS
Crystal Structure Analysis of Low Molecular Weight Protein Tyrosine Phosphatase from T. tengcongensis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE AR-NE3A |
| Synchrotron site | Photon Factory |
| Beamline | AR-NE3A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-03-11 |
| Detector | ADSC QUANTUM 270 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 35.964, 33.176, 117.410 |
| Unit cell angles | 90.00, 90.05, 90.00 |
Refinement procedure
| Resolution | 19.167 - 2.300 |
| R-factor | 0.1953 |
| Rwork | 0.193 |
| R-free | 0.21160 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1zgg |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.862 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((phenix.refine: 1.7.3_928)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.500 | 2.300 |
| High resolution limit [Å] | 2.250 | 2.250 |
| Number of reflections | 13331 | |
| Completeness [%] | 98.5 | 98.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 289 | 25% PEG 3350, 0.1M BIS-TRIS, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
