6ANW
Crystal structure of anti-CRISPR protein AcrF10
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-10-25 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9792 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 73.774, 106.618, 95.349 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.675 - 2.486 |
R-factor | 0.2202 |
Rwork | 0.218 |
R-free | 0.26910 |
Structure solution method | SAD |
RMSD bond length | 0.005 |
RMSD bond angle | 0.642 |
Data scaling software | HKL-2000 |
Phasing software | AutoSol |
Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.590 |
High resolution limit [Å] | 2.500 | 5.380 | 2.500 |
Rmerge | 0.113 | 0.096 | 0.458 |
Rmeas | 0.128 | 0.110 | 0.523 |
Rpim | 0.060 | 0.052 | 0.246 |
Total number of observations | 57879 | ||
Number of reflections | 13323 | 1407 | 1299 |
<I/σ(I)> | 7.6 | ||
Completeness [%] | 98.9 | 97.9 | 99.2 |
Redundancy | 4.3 | 4.2 | 4.2 |
CC(1/2) | 0.990 | 0.855 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 7.5 | 293 | 0.1 M HEPES (pH 7.5) and 1.4 M tri-sodium citrate |