5ELA
The structure of DHAR1 from Arabidopsis thaliana
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I24 |
| Synchrotron site | Diamond |
| Beamline | I24 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-05-21 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 63.690, 63.690, 266.350 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 54.010 - 2.280 |
| R-factor | 0.18374 |
| Rwork | 0.182 |
| R-free | 0.22366 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5el8 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.569 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.2.17) |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 54.010 | 2.340 |
| High resolution limit [Å] | 2.280 | 2.280 |
| Rmerge | 0.043 | 0.635 |
| Number of reflections | 15525 | |
| <I/σ(I)> | 35.9 | 5.1 |
| Completeness [%] | 99.7 | 99.6 |
| Redundancy | 18.1 | 19.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | Protein at 20 mg/ml, 20% PEG 8000, 0.2 M NaK Phosphate, 0.1M TRIS |
