8JFO
Crystal structure of anti-CRISPR protein AcrIIA15
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL02U1 |
| Synchrotron site | SSRF |
| Beamline | BL02U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-08-28 |
| Detector | DECTRIS EIGER2 S 9M |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 41 |
| Unit cell lengths | 88.194, 88.194, 145.649 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 34.680 - 2.300 |
| R-factor | 0.2225 |
| Rwork | 0.222 |
| R-free | 0.23270 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | previously solved AcrIIA15(CTD) structure using SAD |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.307 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.680 | 2.340 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Number of reflections | 49185 | 2431 |
| <I/σ(I)> | 21.6 | |
| Completeness [%] | 99.7 | |
| Redundancy | 5.8 | |
| CC(1/2) | 0.996 | 0.645 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 289 | 0.2 M Trimethylamine N-oxide dihydrate, 0.1 M Tris pH 8.82, 18% w/v PEG 2,000 |






