6X8W
Structure of ArrX Y138A mutant protein bound to sulfate from Chrysiogenes arsenatis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-04-17 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9537 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 53.153, 53.492, 90.184 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.008 - 1.972 |
| Rwork | 0.175 |
| R-free | 0.20700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6x6b |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.434 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0253) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.010 | 2.020 |
| High resolution limit [Å] | 1.970 | 1.970 |
| Number of reflections | 18755 | 1266 |
| <I/σ(I)> | 11 | |
| Completeness [%] | 99.8 | |
| Redundancy | 6.6 | |
| CC(1/2) | 0.999 | 0.802 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.7 | 293 | 0.2 M lithium sulfate, 0.1 M Tris pH 8.7, 27% (w/v) PEG 3350 |
