9BKI
Crystal structure of Rid family protein ACIAD3089 from Acinetobacter baylyi in C2 space group
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-04-21 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.0 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 159.270, 77.380, 150.400 |
Unit cell angles | 90.00, 97.42, 90.00 |
Refinement procedure
Resolution | 43.530 - 2.380 |
R-factor | 0.2013 |
Rwork | 0.200 |
R-free | 0.24290 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.109 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX (1.21_5207) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.440 |
High resolution limit [Å] | 2.380 | 2.380 |
Rmerge | 0.077 | 0.581 |
Number of reflections | 70631 | 4701 |
<I/σ(I)> | 14.85 | 3.88 |
Completeness [%] | 99.4 | |
Redundancy | 6.94 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 298 | 20% PEG 3350, 0.2M SODIUM SULFATE |