6D65
Crystal structure of the human dual specificity phosphatase 1 catalytic domain (C258S) as a maltose binding protein fusion in complex with the designed AR protein off7
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-BM |
| Synchrotron site | APS |
| Beamline | 22-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-10-30 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 75.327, 109.503, 218.558 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.675 - 2.348 |
| R-factor | 0.1879 |
| Rwork | 0.185 |
| R-free | 0.24090 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3h4z 3ezz 1svx |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.895 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.380 |
| High resolution limit [Å] | 2.340 | 2.340 |
| Rmerge | 0.117 | 0.763 |
| Number of reflections | 75855 | 3726 |
| <I/σ(I)> | 17.1 | 2.3 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 4.9 | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 292 | 0.15 M NaCl 0.1 M sodium cacodylate 2.0 M ammonium sulfate |
