1OES
Oxidation state of protein tyrosine phosphatase 1B
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX14.1 |
| Synchrotron site | SRS |
| Beamline | PX14.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC CCD |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 87.686, 87.686, 103.721 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 76.700 - 2.200 |
| R-factor | 0.185 |
| Rwork | 0.182 |
| R-free | 0.23300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1c83 |
| RMSD bond length | 0.009 * |
| RMSD bond angle | 1.400 * |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.29) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 76.000 | 2.320 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.050 | 0.260 |
| Total number of observations | 83434 * | |
| Number of reflections | 23591 | |
| <I/σ(I)> | 7.8 | 2.8 |
| Completeness [%] | 98.9 | 97.4 |
| Redundancy | 3.5 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 | 4 * | Barford, D., (1994) J. Mol. Biol., 239, 726. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | PTP1B | 10 (mg/ml) | |
| 2 | 1 | reservoir | HEPES | 0.1 (M) | |
| 3 | 1 | reservoir | magnesium acetate | 0.2 (M) | |
| 4 | 1 | reservoir | PEG8000 | 12-16 (%(w/v)) |
