7VLM
crystal structure of anti-CRISPR protein AcrIIA18
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 | 2020-12-24 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.979 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 105.371, 32.405, 62.594 |
Unit cell angles | 90.00, 120.37, 90.00 |
Refinement procedure
Resolution | 31.130 - 1.380 |
R-factor | 0.1832 |
Rwork | 0.182 |
R-free | 0.20230 |
Structure solution method | SAD |
RMSD bond length | 0.009 |
RMSD bond angle | 1.190 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHENIX |
Refinement software | PHENIX (1.19rc6_4061) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.430 |
High resolution limit [Å] | 1.380 | 1.380 |
Number of reflections | 37360 | 3705 |
<I/σ(I)> | 16.24 | |
Completeness [%] | 98.5 | |
Redundancy | 3.7 | |
CC(1/2) | 0.991 | 0.905 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | LIQUID DIFFUSION | 291.15 | PEG 3350, calcium acetate |