9L4O
Arabidopsis thaliana protease-associated domain of vacuolar sorting receptor 1 in complexed with vicilin-like seed storage protein 22 C-terminal pentapeptide SDRFV (pH 5.8)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E SUPERBRIGHT |
| Temperature [K] | 93 |
| Detector technology | PIXEL |
| Collection date | 2023-05-12 |
| Detector | DECTRIS EIGER R 4M |
| Wavelength(s) | 1.5419 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 32.658, 60.384, 39.245 |
| Unit cell angles | 90.00, 113.38, 90.00 |
Refinement procedure
| Resolution | 30.190 - 1.900 |
| R-factor | 0.1708 |
| Rwork | 0.169 |
| R-free | 0.21570 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.807 |
| Data reduction software | XDS (VERSION Jan 10, 2022 BUILT=20220820) |
| Data scaling software | Aimless |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.21 1-5286) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 36.020 | 1.940 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Number of reflections | 10890 | 2236 |
| <I/σ(I)> | 19 | |
| Completeness [%] | 98.2 | |
| Redundancy | 3.7 | |
| CC(1/2) | 0.999 | 0.885 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.8 | 289.15 | 0.1 M MES pH 5.8 30% (w/v) PEG 6000 |






