8BEN
LRR domain Structure of the LRRC8C protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 80 |
| Detector technology | PIXEL |
| Collection date | 2017-02-23 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 73.376, 104.726, 111.829 |
| Unit cell angles | 90.00, 94.71, 90.00 |
Refinement procedure
| Resolution | 49.190 - 3.100 |
| R-factor | 0.2438 |
| Rwork | 0.241 |
| R-free | 0.28960 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6fnw |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.841 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.190 | 3.200 |
| High resolution limit [Å] | 3.100 | 3.100 |
| Rmerge | 0.350 | |
| Number of reflections | 30438 | 2773 |
| <I/σ(I)> | 5.53 | |
| Completeness [%] | 98.3 | |
| Redundancy | 7.2 | |
| CC(1/2) | 0.760 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 277.15 | 0.2 M magnesium chloride, 20% PEG3350 |
