2J82
Structural analysis of the PP2C Family Phosphatase tPphA from Thermosynechococcus elongatus
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | MPG/DESY, HAMBURG BEAMLINE BW6 |
Synchrotron site | MPG/DESY, HAMBURG |
Beamline | BW6 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Wavelength(s) | 0.95,0.9796,1.05 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 38.216, 151.799, 82.505 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 75.810 - 1.280 |
R-factor | 0.1633 |
R-free | 0.20420 |
Structure solution method | MAD |
Starting model (for MR) | NONE |
RMSD bond length | 0.013 |
RMSD bond angle | 0.036 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SHELXCD |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 75.810 | 1.370 |
High resolution limit [Å] | 1.280 | 1.280 |
Rmerge | 0.020 | 0.260 |
Number of reflections | 61884 | |
<I/σ(I)> | 25.01 | 3.32 |
Completeness [%] | 99.2 | 98 |
Redundancy | 0.99 | 0.98 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 0.2 M CACL2, 0.1 M HEPES PH 8.0, 28% PEG 3350 |