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 |
