6AS4
Structure of a phage anti-CRISPR protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08B1-1 |
| Synchrotron site | CLSI |
| Beamline | 08B1-1 |
| Temperature [K] | 105 |
| Detector technology | CCD |
| Collection date | 2015-06-10 |
| Detector | RAYONIX MX300HE |
| Wavelength(s) | 0.9793 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 96.740, 63.530, 59.460 |
| Unit cell angles | 90.00, 100.34, 90.00 |
Refinement procedure
| Resolution | 47.585 - 2.000 |
| R-factor | 0.1915 |
| Rwork | 0.190 |
| R-free | 0.22840 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | AcrE1_CHis |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.928 |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.585 | 2.071 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.103 | 1.596 |
| Number of reflections | 23742 | |
| <I/σ(I)> | 11.2 | 1.57 |
| Completeness [%] | 98.5 | 97.59 |
| Redundancy | 7.7 | 7.7 |
| CC(1/2) | 0.529 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 0.2M ammonium citrate dibasic, 20% PEG3350 |
