5W7B
Rabbit acyloxyacyl hydrolase (AOAH), proteolytically processed, S262A 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 | 2016-09-17 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.9801 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 109.522, 138.806, 89.530 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 44.765 - 1.900 |
R-factor | 0.1855 |
Rwork | 0.185 |
R-free | 0.21340 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 0.982 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((1.10.1_2155)) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 1.900 |
Number of reflections | 106913 |
<I/σ(I)> | 19.5 |
Completeness [%] | 100.0 |
Redundancy | 14.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | post-trypsin; 1 mM Triton X-100, 0.333 mM E. coli LPS Ra; 100 mM sodium MES pH 6; 34 % PEG 200; 5 % PEG 3000 |