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 |