6UCC
Structure of human PACRG-MEIG1 complex (limited proteolysis)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08ID-1 |
| Synchrotron site | CLSI |
| Beamline | 08ID-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-07-07 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.9795 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 66.854, 66.854, 158.920 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.270 - 2.600 |
| R-factor | 0.2173 |
| Rwork | 0.214 |
| R-free | 0.28410 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6ndu |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.883 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.15.2_3472) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.270 | 2.720 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.283 | 2.868 |
| Rmeas | 0.295 | 3.131 |
| Rpim | 0.082 | 0.871 |
| Number of reflections | 11793 | 1395 |
| <I/σ(I)> | 9.1 | 1.1 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 12.6 | 12.7 |
| CC(1/2) | 0.996 | 0.557 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 283 | 20% glycerol, 0.2M KH2PO4, 20% PEG 8000 |






