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) |






