7E0C
Structure of L-glutamate oxidase R305E mutant
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 | 2016-10-08 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 123.970, 123.970, 168.631 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 66.311 - 2.650 |
| R-factor | 0.1934 |
| Rwork | 0.191 |
| R-free | 0.24090 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2e1m |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.860 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.15.2_3472: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 84.300 | 2.780 |
| High resolution limit [Å] | 2.650 | 2.650 |
| Rmerge | 0.115 | 0.670 |
| Rpim | 0.034 | 0.191 |
| Number of reflections | 22897 | 2970 |
| <I/σ(I)> | 18.5 | 4.6 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 12.3 | 13 |
| CC(1/2) | 0.999 | 0.930 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 277 | 12% (w/v) PEG 8000, 0.1M Tris-HCl pH7.0, 75mM MgCl2 |






