5IXT
The crystal structure of the Arabidopsis receptor kinase HAESA LRR ectdomain in complex with a N-terminal extended IDA peptide hormone ligand.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-05-15 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.999980 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 148.921, 148.921, 58.022 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 128.970 - 1.940 |
| R-factor | 0.18068 |
| Rwork | 0.179 |
| R-free | 0.20763 |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | 5ixo |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.800 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 128.970 | 2.060 |
| High resolution limit [Å] | 1.940 | 1.940 |
| Number of reflections | 54201 | |
| <I/σ(I)> | 20.9 | 2.4 |
| Completeness [%] | 99.4 | 97.9 |
| Redundancy | 11.2 | 11.1 |
| CC(1/2) | 1.000 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4 | 298 | 23% PEG 3350,0.2M MgCl2,0.1M citric acid pH4 |
