6AS3
Structure of a phage anti-CRISPR protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 105 |
| Detector technology | CCD |
| Collection date | 2014-11-01 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 61.799, 87.462, 91.102 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 63.090 - 2.000 |
| R-factor | 0.1666 |
| Rwork | 0.164 |
| R-free | 0.21410 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6arz |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.877 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 63.090 | 2.071 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 1.363 | |
| Number of reflections | 34051 | 3351 |
| <I/σ(I)> | 18.91 | 3.97 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 9.2 | 8.3 |
| CC(1/2) | 0.703 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 0.1M Tris pH 7.0, 20% PEG 3350 |
