6IHT
Crystal structure of bacterial serine phosphatase bound with phosphorylated peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL18U1 |
| Synchrotron site | SSRF |
| Beamline | BL18U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-12-12 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.9735 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 46.693, 38.609, 65.003 |
| Unit cell angles | 90.00, 101.89, 90.00 |
Refinement procedure
| Resolution | 45.692 - 1.569 |
| R-factor | 0.1602 |
| Rwork | 0.159 |
| R-free | 0.18340 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5f1m |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.290 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.630 |
| High resolution limit [Å] | 1.569 | 1.570 |
| Rmerge | 0.087 | 0.370 |
| Number of reflections | 31706 | 3198 |
| <I/σ(I)> | 39.5 | |
| Completeness [%] | 99.2 | |
| Redundancy | 6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 289 | 0.05 M MgCl2, 0.1 M HEPES (pH=7.5), 30% PEG 3350. |
