5LNM
Crystal structure of D1050E mutant of the receiver domain of the histidine kinase CKI1 from Arabidopsis thaliana
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X12 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X12 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-11-06 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.975220 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 54.337, 98.728, 79.897 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 42.370 - 1.950 |
| R-factor | 0.20848 |
| Rwork | 0.207 |
| R-free | 0.23381 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3mm4 |
| RMSD bond length | 0.019 |
| RMSD bond angle | 2.037 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.600 | 2.060 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.117 | 0.665 |
| Number of reflections | 15893 | |
| <I/σ(I)> | 10.8 | 1.6 |
| Completeness [%] | 99.2 | 94.8 |
| Redundancy | 5.7 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.05 | 290.15 | 2.54 M (NH4)2(SO4), 0.1 M MES pH 5.05 |
