7C3J
Structure of L-lysine oxidase D212A/D315A in complex with L-phenylalanine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL41XU |
| Synchrotron site | SPring-8 |
| Beamline | BL41XU |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-11-23 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.000 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 114.920, 169.680, 118.530 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 68.990 - 2.200 |
| R-factor | 0.1884 |
| Rwork | 0.186 |
| R-free | 0.23560 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3x0v |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.635 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.15.2_3472) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 95.200 | 2.260 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.101 | 0.298 |
| Number of reflections | 58372 | 4495 |
| <I/σ(I)> | 7 | 3.3 |
| Completeness [%] | 99.1 | 98.7 |
| Redundancy | 4.4 | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 1% (w/v) PEG 400, 0.1 M Tris-HCl pH 7.5, 2.1 M Ammonium Sulfate |
