2HWN
Crystal Structure of RII alpha Dimerization/Docking domain of PKA bound to the D-AKAP2 peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.3 |
Synchrotron site | ALS |
Beamline | 5.0.3 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-11-20 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1.0 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 99.551, 44.561, 72.802 |
Unit cell angles | 90.00, 124.07, 90.00 |
Refinement procedure
Resolution | 30.500 - 1.600 |
R-factor | 0.20823 |
Rwork | 0.208 |
R-free | 0.23900 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.012 |
RMSD bond angle | 1.320 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.500 | 1.660 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.045 | 0.414 |
Number of reflections | 29191 | |
<I/σ(I)> | 36.9 | 3.6 |
Completeness [%] | 87.7 | 99.9 |
Redundancy | 6.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | 100mM HEPES, 20% PEG 8000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |