5W7C
Human acyloxyacyl hydrolase (AOAH), proteolytically processed, S263A mutant, with LPS
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08ID-1 |
| Synchrotron site | CLSI |
| Beamline | 08ID-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-05-23 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 0.97243 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 88.170, 104.080, 145.280 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 44.816 - 2.230 |
| R-factor | 0.2132 |
| Rwork | 0.211 |
| R-free | 0.24510 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.621 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10.1_2155)) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 2.230 |
| Number of reflections | 61346 |
| <I/σ(I)> | 9.4 |
| Completeness [%] | 100.0 |
| Redundancy | 13.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | post-chymotrypsin; 1mM Triton X-100, 0.333 mM E. coli LPS Ra; 200 mM ammonium chloride, 100 mM sodium acetate pH 5.3, 20 % PEG 6000 |






