5Y6A
Crystal structure of the anti-CRISPR protein, AcrIIA1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PAL/PLS BEAMLINE 7A (6B, 6C1) |
| Synchrotron site | PAL/PLS |
| Beamline | 7A (6B, 6C1) |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2017-06-22 |
| Detector | ADSC QUANTUM 270 |
| Wavelength(s) | 0.9793 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 127.435, 55.420, 46.504 |
| Unit cell angles | 90.00, 96.01, 90.00 |
Refinement procedure
| Resolution | 28.326 - 2.000 |
| R-factor | 0.1851 |
| Rwork | 0.183 |
| R-free | 0.22840 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5y69 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.902 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.112 | 0.716 |
| Number of reflections | 21982 | |
| <I/σ(I)> | 19.86 | 3.8 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 6.9 | 6.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 293 | 0.1 M Mg Acetate, 13 % (w/v) PEG6000, 0.05 M Na cacodylate pH 6.5 |
