9L2Q
Crystal structure of anti-CRISPR protein AcrIE7
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL19U1 |
Synchrotron site | SSRF |
Beamline | BL19U1 |
Temperature [K] | 80 |
Detector technology | PIXEL |
Collection date | 2020-11-29 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.979 |
Spacegroup name | P 63 2 2 |
Unit cell lengths | 108.714, 108.714, 187.651 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 54.360 - 2.054 |
R-factor | 0.188 |
Rwork | 0.186 |
R-free | 0.22280 |
Structure solution method | SAD |
RMSD bond length | 0.006 |
RMSD bond angle | 0.773 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHENIX |
Refinement software | PHENIX (1.20_4459) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 54.360 | 2.218 |
High resolution limit [Å] | 2.054 | 2.054 |
Number of reflections | 33956 | 34003 |
<I/σ(I)> | 34.94 | |
Completeness [%] | 81.7 | |
Redundancy | 1.9 | |
CC(1/2) | 1.000 | 0.846 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | LIQUID DIFFUSION | 291.15 | PEG 8000,HEPES/ Sodkum hydroxide |