7C78
The crystal structure of type I-F anti-crispr protein AcrIF9
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL19U1 |
Synchrotron site | SSRF |
Beamline | BL19U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2019-01-03 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.979 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 47.899, 57.806, 27.299 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 36.880 - 1.980 |
R-factor | 0.2113 |
Rwork | 0.210 |
R-free | 0.23700 |
Structure solution method | SAD |
RMSD bond length | 0.002 |
RMSD bond angle | 0.466 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AutoSol |
Refinement software | PHENIX (1.17.1_3660) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.050 |
High resolution limit [Å] | 1.980 | 1.980 |
Rmerge | 0.150 | 0.599 |
Number of reflections | 10105 | 512 |
<I/σ(I)> | 22.46 | |
Completeness [%] | 99.1 | |
Redundancy | 16.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 291 | PEG4000 |