6IUF
Crystal structure of Anti-CRISPR protein AcrVA5
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U1 |
| Synchrotron site | SSRF |
| Beamline | BL17U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-09-28 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 41 3 2 |
| Unit cell lengths | 143.422, 143.422, 143.422 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.807 - 2.052 |
| R-factor | 0.1541 |
| Rwork | 0.152 |
| R-free | 0.18640 |
| Structure solution method | SAD |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.683 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.090 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.052 | |
| Number of reflections | 32118 | |
| <I/σ(I)> | 52.1 | |
| Completeness [%] | 99.9 | |
| Redundancy | 11.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.1 | 293 | 0.1M NaAc, 2M (NH4)2SO4, pH 5.1 |






