3TNQ
Structure and Allostery of the PKA RIIb Tetrameric Holoenzyme
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.2 |
Synchrotron site | ALS |
Beamline | 8.2.2 |
Temperature [K] | 200 |
Detector technology | CCD |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1 |
Spacegroup name | C 2 2 2 |
Unit cell lengths | 153.819, 212.753, 61.951 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.836 - 3.097 |
R-factor | 0.2335 |
Rwork | 0.231 |
R-free | 0.27530 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.016 |
RMSD bond angle | 1.552 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX ((phenix.refine: 1.6.1_357)) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 40.000 |
High resolution limit [Å] | 3.097 |
Number of reflections | 16119 |
Completeness [%] | 90.0 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | The RII (R230K)2:C2 holoenzyme complex was crystallized at room temperature in 10% PEG8000, 8% ethylene glycol, pH7.5 HEPES buffer by using vapor diffusion at a 1:1 ratio of protein to crystallization solution. VAPOR DIFFUSION, HANGING DROP, temperature 298K |