5VR6
Structure of Human Sts-1 histidine phosphatase domain with sulfate bound
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-04-13 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 0.97910 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 62.640, 79.160, 105.102 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.870 |
| R-factor | 0.19655 |
| Rwork | 0.194 |
| R-free | 0.24101 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2h0q |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.115 |
| Data reduction software | d*TREK |
| Data scaling software | d*TREK |
| 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 | 1.900 |
| High resolution limit [Å] | 1.870 | 5.070 | 1.870 |
| Rmerge | 0.077 | 0.041 | 0.203 |
| Rmeas | 0.086 | 0.046 | 0.232 |
| Rpim | 0.037 | 0.020 | 0.109 |
| Total number of observations | 211226 | ||
| Number of reflections | 41518 | ||
| <I/σ(I)> | 4.9 | ||
| Completeness [%] | 94.4 | 99.3 | 77.7 |
| Redundancy | 5.1 | 5 | 4.1 |
| CC(1/2) | 0.998 | 0.973 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 291 | 22 - 25% PEG 2000 MME 200 mM Ammonium Sulfate 0.1 M Sodium Acetate |
