9W56
Structure of L-glutamate oxidase E617Q mutant in complex with L-glutamate
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 | 2022-01-21 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 85.957, 117.651, 147.953 |
| Unit cell angles | 90.00, 105.16, 90.00 |
Refinement procedure
| Resolution | 61.040 - 2.380 |
| R-factor | 0.1766 |
| Rwork | 0.174 |
| R-free | 0.22020 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2e1m |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.609 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.21.2_5419) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 71.400 | 2.420 |
| High resolution limit [Å] | 2.380 | 2.380 |
| Number of reflections | 111889 | 5529 |
| <I/σ(I)> | 5.6 | 2.3 |
| Completeness [%] | 98.3 | 95 |
| Redundancy | 3.3 | 3.3 |
| CC(1/2) | 0.983 | 0.805 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 0.1 M Tris-HCl (pH 7.0), 12% (w/v) PEG8000, and 0.2 M MgCl2 |
