8B28
Structure of an intron-retention variant of the plant immune signalling protein EDS1 from Vitis vinifera
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID30B |
| Synchrotron site | ESRF |
| Beamline | ID30B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-02-26 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.915079 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 144.549, 65.077, 45.454 |
| Unit cell angles | 90.00, 105.48, 90.00 |
Refinement procedure
| Resolution | 43.810 - 1.750 |
| R-factor | 0.1755 |
| Rwork | 0.174 |
| R-free | 0.20590 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6i8g |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.567 |
| Data reduction software | XDS (Jan 10, 2022 (BUILT 20220820)) |
| Data scaling software | autoPROC (1.0.5) |
| Phasing software | PHENIX (1.20.1_4487) |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.810 | 1.942 |
| High resolution limit [Å] | 1.750 | 1.755 |
| Rmerge | 0.106 | 0.668 |
| Number of reflections | 29029 | 1451 |
| <I/σ(I)> | 5.7 | 1.4 |
| Completeness [%] | 71.3 | |
| Redundancy | 2.8 | |
| CC(1/2) | 0.988 | 0.658 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | Protein solution: 4.5 mg/ml in 300 mM sodium iodide, 1 % glycerol, 1 mM DTT, 50 mM Hepes buffer, pH 8.0). Reservoir solution: 12 % PEG3350, 300 millimolar CsCl, 100 millimolar Bis-Tris puffer, pH 8.5. Crystallization drop before equilibration: 1.5 mikroliter protein solution plus and 1.5 mikroliter reservoir solution. |






