7D4C
Structure of L-lysine oxidase precursor
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 | 2017-04-19 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 1.000 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 95.160, 130.920, 94.070 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 76.975 - 1.970 |
R-factor | 0.2044 |
Rwork | 0.203 |
R-free | 0.23460 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3x0v |
RMSD bond length | 0.003 |
RMSD bond angle | 0.821 |
Data reduction software | iMOSFLM |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 94.100 | 2.020 |
High resolution limit [Å] | 1.970 | 1.970 |
Rmerge | 0.106 | 0.527 |
Rpim | 0.080 | 0.284 |
Number of reflections | 39115 | 2880 |
<I/σ(I)> | 10.3 | 2.9 |
Completeness [%] | 93.5 | 99.9 |
Redundancy | 5 | 5.2 |
CC(1/2) | 0.978 | 0.810 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 0.1 M Tris-HCl pH8.5 and 2.0 M ammonium dihydrogen phosphate |