5ZNE
The crystal structure of immune receptor RGA5A_S of resistance protein Pia from rice (Oryza sativa)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U1 |
| Synchrotron site | SSRF |
| Beamline | BL17U1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2015-09-10 |
| Detector | MAC Science DIP-320 |
| Wavelength(s) | 0.9795 |
| Spacegroup name | P 43 2 2 |
| Unit cell lengths | 55.619, 55.619, 78.335 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.350 - 1.780 |
| R-factor | 0.2189 |
| Rwork | 0.218 |
| R-free | 0.23760 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3dxs |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.805 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.12_2829: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 55.080 | 2.314 |
| High resolution limit [Å] | 1.780 | 2.234 |
| Rmerge | 0.012 | |
| Rmeas | 0.017 | |
| Number of reflections | 21743 | 6259 |
| <I/σ(I)> | 20.05 | |
| Completeness [%] | 99.8 | 99.84 |
| Redundancy | 2 | 2 |
| CC(1/2) | 1.000 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 289 | 0.18 M ammonium nitrate 20% PEG3350 |






