3ICF
Structure of Protein serine/threonine phosphatase from Saccharomyces cerevisiae with similarity to human phosphatase PP5
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-12-17 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97926 |
| Spacegroup name | P 32 |
| Unit cell lengths | 47.194, 47.194, 237.096 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 40.290 - 2.300 |
| R-factor | 0.19244 |
| Rwork | 0.190 |
| R-free | 0.23994 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1wao |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.547 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.290 | 2.380 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.077 | 0.301 |
| Number of reflections | 25761 | |
| <I/σ(I)> | 29.286 | 3.5 |
| Completeness [%] | 97.9 | 82.9 |
| Redundancy | 5.5 | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 294 | 0.1 M Hepes 7.5, 0.2 M NaCl, 25% PEG3350 plus 0.015 mg/ml V8 protease. Cryoprotected with Paratone-N oil, VAPOR DIFFUSION, SITTING DROP, temperature 294K |
