9LGR
Y-degron fused ZZ-domain of the Arabidopsis thaliana E3 ubiquitin-protein ligase BIG
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PAL/PLS BEAMLINE 5C (4A) |
| Synchrotron site | PAL/PLS |
| Beamline | 5C (4A) |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-05-17 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 1 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 23.781, 93.830, 80.876 |
| Unit cell angles | 90.00, 92.86, 90.00 |
Refinement procedure
| Resolution | 30.610 - 2.050 |
| R-factor | 0.1945 |
| Rwork | 0.192 |
| R-free | 0.21870 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.887 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.18rc7_3834) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.090 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.155 | 0.475 |
| Number of reflections | 21444 | 1973 |
| <I/σ(I)> | 14.7 | |
| Completeness [%] | 97.2 | |
| Redundancy | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 1.4 M NaHPO4/KH2PO4 pH 7.0 |
