6IHU
Crystal structure of bacterial serine phosphatase bearing R161A mutation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL19U1 |
Synchrotron site | SSRF |
Beamline | BL19U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-11-30 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.9735 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 46.998, 37.745, 65.575 |
Unit cell angles | 90.00, 102.87, 90.00 |
Refinement procedure
Resolution | 29.475 - 1.840 |
R-factor | 0.1705 |
Rwork | 0.169 |
R-free | 0.20040 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5f1m |
RMSD bond length | 0.003 |
RMSD bond angle | 0.593 |
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] | 30.000 | 1.920 |
High resolution limit [Å] | 1.840 | 1.840 |
Rmerge | 0.100 | 0.272 |
Number of reflections | 18646 | 1702 |
<I/σ(I)> | 12.3 | |
Completeness [%] | 95.4 | |
Redundancy | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 289 | 0.2 M NaCl, 0.1 M HEPES (pH=7.5), 25% PEG 3350. |