6C6K
Structural basis for preferential recognition of cap 0 RNA by a human IFIT1-IFIT3 protein complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 80 |
| Detector technology | CCD |
| Collection date | 2016-12-02 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97957 |
| Spacegroup name | P 1 |
| Unit cell lengths | 51.957, 80.484, 88.054 |
| Unit cell angles | 79.82, 78.81, 90.04 |
Refinement procedure
| Resolution | 84.960 - 2.540 |
| R-factor | 0.1722 |
| Rwork | 0.169 |
| R-free | 0.23670 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.668 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER (2.7.17) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 84.960 | 50.000 | 2.590 |
| High resolution limit [Å] | 2.540 | 6.920 | 2.550 |
| Rmerge | 0.076 | 0.055 | 0.326 |
| Rmeas | 0.090 | 0.065 | 0.394 |
| Rpim | 0.047 | 0.034 | 0.219 |
| Number of reflections | 41031 | 2128 | 1762 |
| <I/σ(I)> | 10.1 | ||
| Completeness [%] | 90.9 | 94.1 | 75.6 |
| Redundancy | 3.4 | 3.6 | 2.9 |
| CC(1/2) | 0.944 | 0.867 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 6.4 | 293 | imidazole, PEG20000 |






