9AVH
Crystal structure of an aryl-alcohol-oxidase from Bjerkandera adusta.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALBA BEAMLINE XALOC |
Synchrotron site | ALBA |
Beamline | XALOC |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-03-07 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.979257 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 56.035, 82.746, 116.837 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 67.526 - 1.800 |
Rwork | 0.143 |
R-free | 0.18830 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.665 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0419) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 116.840 | 1.900 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.097 | 0.843 |
Number of reflections | 50514 | 7207 |
<I/σ(I)> | 12.2 | 2.7 |
Completeness [%] | 98.9 | 98.2 |
Redundancy | 6.7 | 6.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 291 | 12% v/v glycerol, 1.5 M ammonium sulfate, 0.1 mM Tris/HCl, pH 8.5 |