5YHR
Crystal structure of the anti-CRISPR protein, AcrF2
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 | 2017-09-13 |
| Detector | ADSC QUANTUM 270 |
| Wavelength(s) | 0.97929 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 65.546, 65.546, 101.327 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 23.174 - 1.340 |
| R-factor | 0.1802 |
| Rwork | 0.180 |
| R-free | 0.19620 |
| Structure solution method | SAD |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.961 |
| 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 | 1.390 |
| High resolution limit [Å] | 1.340 | 1.340 |
| Rmerge | 0.102 | 0.582 |
| Rmeas | 0.104 | 0.594 |
| Rpim | 0.020 | 0.117 |
| Number of reflections | 50291 | 4925 |
| <I/σ(I)> | 29.79 | 6.43 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 27.9 | 25.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 293 | 21% (w/v) PEG 6000, 0.4 M CaCl2, 100 mM MES pH 5.5 |
