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 |