3C5W
Complex between PP2A-specific methylesterase PME-1 and PP2A core enzyme
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 | 2007-09-10 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0809 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 129.292, 54.839, 125.146 |
Unit cell angles | 90.00, 110.87, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.800 |
R-factor | 0.19844 |
Rwork | 0.195 |
R-free | 0.26338 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PP2A A subunit PP2A C subunit PME-1 monomer |
RMSD bond length | 0.007 |
RMSD bond angle | 1.087 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.3.0038) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Number of reflections | 20623 | |
Completeness [%] | 98.6 | 95.7 |
Redundancy | 3 | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 290 | 25% w/v PEG3350, 100 mM ammonium citrate, and 5 mM DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K |