2I4H
Structural studies of protein tyrosine phosphatase beta catalytic domain co-crystallized with a sulfamic acid inhibitor
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 | 2005-03-03 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.0 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 113.313, 38.795, 66.983 |
| Unit cell angles | 90.00, 104.94, 90.00 |
Refinement procedure
| Resolution | 27.370 - 2.150 |
| R-factor | 0.17 |
| Rwork | 0.169 |
| R-free | 0.24600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2hc1 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.843 |
| 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] | 27.370 | 2.250 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmerge | 0.063 | 0.187 |
| Number of reflections | 15799 | |
| <I/σ(I)> | 12.48 | 5.26 |
| Completeness [%] | 99.5 | 97.2 |
| Redundancy | 4 | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.1 | 298 | 20% PEG 8000, 220 mM MgCl2, 80 mM NH4OAc, 1% BME, 0.1% BOG, 5mM DTT, pH 8.1, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
