5EL8
The structure of DHAR1 from Arabidopsis thaliana
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I02 |
| Synchrotron site | Diamond |
| Beamline | I02 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-03-08 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 64.900, 64.900, 259.000 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 56.200 - 2.300 |
| R-factor | 0.20505 |
| Rwork | 0.203 |
| R-free | 0.23616 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1k0o |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.593 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.2.17) |
| Phasing software | PHASER (2.2.1) |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 56.200 | 2.350 |
| High resolution limit [Å] | 2.300 | 2.280 |
| Rmerge | 0.132 | 0.800 |
| Number of reflections | 15743 | |
| <I/σ(I)> | 6.1 | 1 |
| Completeness [%] | 99.9 | 99.8 |
| Redundancy | 5.4 | 5.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | Protein at 20mg/ml concentration 20% PEG 8000, 0.2M NaK Phosphate, 0.1M Tris |
