2NPP
Structure of the Protein Phosphatase 2A Holoenzyme
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-10-09 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9793 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 109.260, 159.050, 269.170 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 100.000 - 3.300 |
R-factor | 0.26 |
Rwork | 0.255 |
R-free | 0.29900 |
Structure solution method | combined with Molecular Replacement |
RMSD bond length | 0.008 |
RMSD bond angle | 1.380 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 3.420 |
High resolution limit [Å] | 3.300 | 3.300 |
Rmerge | 0.104 | |
Number of reflections | 70289 | |
Completeness [%] | 99.9 | 99.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 277.5 | 15% PEG 8000, 0.1 M Tris-Cl pH 8.5, and 0.2 M magnesium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 277.5K |