3I36
Crystal Structure of Rat Protein Tyrosine Phosphatase eta Catalytic Domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | LNLS BEAMLINE D03B-MX1 |
| Synchrotron site | LNLS |
| Beamline | D03B-MX1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-01-01 |
| Detector | MAR CCD 165 mm |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 46.468, 63.113, 111.655 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.715 - 1.841 |
| R-factor | 0.1592 |
| Rwork | 0.157 |
| R-free | 0.20230 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ahs |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.237 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.420 | 1.940 |
| High resolution limit [Å] | 1.840 | 1.840 |
| Rmerge | 0.058 | 0.238 |
| Number of reflections | 28395 | |
| <I/σ(I)> | 9.1 | 4.5 |
| Completeness [%] | 97.6 | 95 |
| Redundancy | 3.5 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 291 | 20% PEG 10000, 0.1M MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
