5H78
Crystal structure of the PKA-DHR14 fusion protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 7A (6B, 6C1) |
Synchrotron site | PAL/PLS |
Beamline | 7A (6B, 6C1) |
Temperature [K] | 80 |
Detector technology | CCD |
Collection date | 2016-06-29 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.97934 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 179.234, 96.539, 39.351 |
Unit cell angles | 90.00, 89.90, 90.00 |
Refinement procedure
Resolution | 29.593 - 2.002 |
R-factor | 0.1822 |
Rwork | 0.181 |
R-free | 0.20680 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2izx 5cwh |
RMSD bond length | 0.009 |
RMSD bond angle | 0.857 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 83181 | |
<I/σ(I)> | 19.8 | 4.21 |
Completeness [%] | 98.7 | 99.5 |
Redundancy | 3.5 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 6.5 | 296 | 0.05M sodium cacodylate pH 6.5, 0.01M magnesium chloride, 0.2M potassium chloride, 12%(w/v) PEG 4000 |