2I4G
Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with a sulfamic acid (soaking experiment)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-02-02 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 38.852, 69.610, 117.777 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 34.200 - 1.650 |
| R-factor | 0.17 |
| Rwork | 0.176 |
| R-free | 0.22000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2i4e |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.583 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.200 | 1.750 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.038 | 0.330 |
| Number of reflections | 29360 | |
| <I/σ(I)> | 15.1 | 3 |
| Completeness [%] | 73.9 | 39.3 |
| Redundancy | 2.5 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.1 | 298 | 20% PEG 8000, 200 mM MgCl2, 80 mM NH4OAc, 1% BME, 0.1% BOG, 5mM DTT, pH 8.1, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
