2CM1
Crystal structure of the catalytic domain of serine threonine protein phosphatase PstP in complex with 2 Manganese ions.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-02-15 |
Detector | ADSC CCD |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 69.142, 69.142, 89.431 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 59.870 - 2.000 |
R-factor | 0.199 |
Rwork | 0.197 |
R-free | 0.24300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1txo |
RMSD bond length | 0.017 |
RMSD bond angle | 1.750 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 60.000 | 2.200 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.090 | 0.400 |
Number of reflections | 15969 | |
<I/σ(I)> | 11.67 | 3.96 |
Completeness [%] | 92.8 | 84.1 |
Redundancy | 3.5 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 14% PEG 8000, 50MM KH2PO4 PH6.5, 15% GLYCEROL |