2Y96
Structure of human dual-specificity phosphatase 27
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 | 2011-10-14 |
Detector | MARRESEARCH |
Spacegroup name | P 64 2 2 |
Unit cell lengths | 126.012, 126.012, 125.758 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 2.380 |
R-factor | 0.20257 |
Rwork | 0.201 |
R-free | 0.22482 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2pq5 |
RMSD bond length | 0.015 |
RMSD bond angle | 1.514 |
Data reduction software | HKL-3000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0104) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.430 |
High resolution limit [Å] | 2.380 | 2.380 |
Rmerge | 0.070 | 0.720 |
Number of reflections | 24047 | |
<I/σ(I)> | 48.2 | 4.2 |
Completeness [%] | 100.0 | 100 |
Redundancy | 16.1 | 15.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6 | 10 MG/ML PROTEIN, 0.2M AMMONIUM SULFATE, 25% W/V PEG3350, ROOM TEMPERATURE, pH 6 |