3EEH
The crystal structure of the domain of the putative light and redox sensing histidine kinase from Haloarcula marismortui
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-10-05 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9794 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 96.558, 96.558, 40.131 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 83.620 - 1.950 |
| R-factor | 0.18011 |
| Rwork | 0.179 |
| R-free | 0.20057 |
| Structure solution method | SAD |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.835 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.5.0054) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 83.620 | 2.000 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.091 | 0.505 |
| Number of reflections | 15139 | |
| <I/σ(I)> | 51.9 | 3.1 |
| Completeness [%] | 99.8 | 98.45 |
| Redundancy | 12.9 | 8.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 289 | 1.0M LiCl, 0.1M NaCl, 30% PEG6000, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
