5WDI
Structure of Human Sts-2 histidine phosphatase domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-11-08 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 77.507, 113.115, 60.994 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 63.940 - 2.430 |
| R-factor | 0.2058 |
| Rwork | 0.203 |
| R-free | 0.25010 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3d4i |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.006 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.470 |
| High resolution limit [Å] | 2.430 | 6.590 | 2.430 |
| Rmerge | 0.092 | 0.024 | 0.568 |
| Rmeas | 0.107 | 0.029 | 0.671 |
| Rpim | 0.055 | 0.015 | 0.353 |
| Total number of observations | 74181 | ||
| Number of reflections | 20513 | 958 | |
| <I/σ(I)> | 7.7 | ||
| Completeness [%] | 98.3 | 98.9 | 94.2 |
| Redundancy | 3.6 | 3.4 | 3.4 |
| CC(1/2) | 0.999 | 0.745 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 291 | 0.1 M HEPES, pH 7.0 22% PEG 4000 0.2 M potassium acetate 0.2 M lithium sulfate |
