7KLX
Protein Tyrosine Phosphatase 1B with inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 31-ID |
| Synchrotron site | APS |
| Beamline | 31-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-11-13 |
| Detector | MAR CCD 130 mm |
| Wavelength(s) | 0.979290 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 88.300, 88.300, 104.791 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 76.470 - 1.839 |
| R-factor | 0.1967 |
| Rwork | 0.196 |
| R-free | 0.20490 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2cm8 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.950 |
| Data reduction software | XDS (Jan 31, 2020) |
| Data scaling software | Aimless (0.7.4) |
| Phasing software | EPMR |
| Refinement software | BUSTER (2.10.3) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 76.470 | 1.870 |
| High resolution limit [Å] | 1.840 | 1.840 |
| Rpim | 0.016 | 0.325 |
| Number of reflections | 40080 | 2033 |
| <I/σ(I)> | 26.1 | 2.4 |
| Completeness [%] | 96.5 | 100 |
| Redundancy | 10.9 | 11.1 |
| CC(1/2) | 1.000 | 0.811 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.7 | 293 | 12% PEG 3350, 100 mM magnesium acetate, 3% ethanol |
