3OD0
Crystal structure of cGMP bound cGMP-dependent protein kinase(92-227)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.1 |
Synchrotron site | ALS |
Beamline | 8.2.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-07-01 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.000 |
Spacegroup name | P 62 2 2 |
Unit cell lengths | 107.625, 107.625, 171.391 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 48.708 - 2.900 |
R-factor | 0.2064 |
Rwork | 0.204 |
R-free | 0.25980 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.422 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | BALBES |
Refinement software | PHENIX ((phenix.refine: 1.6.2_431)) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.900 |
Rmerge | 0.103 |
Number of reflections | 13503 |
Completeness [%] | 100.0 |
Redundancy | 29.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 277.15 | 0.1M sodium malonate, 12% PEG 3350, 3% D-(+)-glucose monohydrate , pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K |