5C5E
Structure of KaiA dimer in complex with C-terminal KaiC peptide at 2.8 A resolution
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] | 100 |
| Detector technology | CCD |
| Collection date | 2014-06-04 |
| Detector | RAYONIX MX225HE |
| Wavelength(s) | 0.978 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 97.430, 97.430, 124.520 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.192 - 2.820 |
| R-factor | 0.243 |
| Rwork | 0.240 |
| R-free | 0.30290 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4g86 |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.813 |
| Data reduction software | HKL-2000 |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.192 | 2.890 |
| High resolution limit [Å] | 2.820 | 2.820 |
| Rmerge | 0.100 | 0.805 |
| Number of reflections | 15075 | |
| <I/σ(I)> | 37.1 | 4.7 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 22 | 22.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.8 | 289 | 180 mM ammonium sulfate, 85 mM sodium cacodylate pH 6.8, 20% PEG 8000 and 15% glycerol in the reservoir. |
