7EII
Ancestral L-Lys oxidase K387A variant (L-Lys binding form)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-5A |
Synchrotron site | Photon Factory |
Beamline | BL-5A |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-10-23 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 85.829, 80.086, 87.986 |
Unit cell angles | 90.00, 90.42, 90.00 |
Refinement procedure
Resolution | 42.900 - 2.400 |
Rwork | 0.183 |
R-free | 0.23080 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 7eih |
RMSD bond length | 0.007 |
RMSD bond angle | 1.460 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 42.900 | 2.530 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.087 | 0.421 |
Number of reflections | 46762 | 6740 |
<I/σ(I)> | 16.2 | |
Completeness [%] | 99.8 | |
Redundancy | 6.8 | |
CC(1/2) | 0.998 | 0.926 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 295 | 25%(w/v) PEG3350, 0.1 M Tris-HCl (pH 8.5) |