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 |