7E0D
Structure of L-glutamate oxidase R305E mutant in complex with L-arginine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-11-09 |
| Detector | RAYONIX MX225HE |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 124.760, 124.760, 170.201 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 54.000 - 2.700 |
| R-factor | 0.2009 |
| Rwork | 0.198 |
| R-free | 0.25510 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2e1m |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.549 |
| 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] | 54.000 | 2.830 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.178 | 0.699 |
| Rpim | 0.089 | 0.317 |
| Number of reflections | 21123 | 2842 |
| <I/σ(I)> | 7.7 | 2.5 |
| Completeness [%] | 96.4 | 99.1 |
| Redundancy | 4.8 | 4.8 |
| CC(1/2) | 0.981 | 0.744 |
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 |






