3S1A
Crystal structure of the phosphorylation-site double mutant S431E/T432E of the KaiC circadian clock protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 113.15 |
Detector technology | CCD |
Collection date | 2009-01-20 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 132.666, 135.494, 204.603 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 17.000 - 3.000 |
R-factor | 0.268 |
Rwork | 0.242 |
R-free | 0.28800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3dvl |
RMSD bond length | 0.009 |
RMSD bond angle | 1.517 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 17.000 | 3.050 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.075 | 0.381 |
Number of reflections | 73982 | |
<I/σ(I)> | 2.3 | 3.34 |
Completeness [%] | 99.4 | 96 |
Redundancy | 3.9 | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 291 | SODIUM FORMATE, GLYCEROL, pH 5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |