5LNN
Crystal structure of D1050A 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 | 2009-11-05 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.975220 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 53.176, 101.005, 79.464 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 42.510 - 1.600 |
R-factor | 0.19418 |
Rwork | 0.192 |
R-free | 0.22806 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3mm4 |
RMSD bond length | 0.026 |
RMSD bond angle | 2.377 |
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] | 47.050 | 1.690 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.023 | 0.175 |
Number of reflections | 28315 | |
<I/σ(I)> | 37.9 | 5.4 |
Completeness [%] | 98.9 | 95.3 |
Redundancy | 6.4 | 3.6 |
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 |