6GG1
Structure of PROSS-edited human interleukin 24
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-03-08 |
| Detector | DECTRIS PILATUS 2M |
| Wavelength(s) | 0.91841 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 38.920, 65.369, 67.502 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.960 - 1.300 |
| R-factor | 0.1676 |
| Rwork | 0.161 |
| R-free | 0.18345 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1n1f |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.525 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | BALBES |
| Refinement software | REFMAC (5.8.0222) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 46.960 | 46.960 | 1.320 |
| High resolution limit [Å] | 1.300 | 7.120 | 1.300 |
| Rmerge | 0.069 | 0.075 | |
| Rmeas | 0.074 | 0.081 | |
| Rpim | 0.028 | 0.029 | |
| Number of reflections | 43156 | 327 | 2091 |
| <I/σ(I)> | 14.7 | 42.9 | 1.3 |
| Completeness [%] | 100.0 | 99.9 | 99.9 |
| Redundancy | 13 | 11.8 | 11.9 |
| CC(1/2) | 0.999 | 0.997 | 0.610 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 293 | 20% PEG8000, 0.2M CaCl2, 0.1M MES |
