8EYZ
Engineered glutamine binding protein bound to GLN and a cobaloxime ligand
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2022-04-16 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 0.97856 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 75.125, 136.091, 150.980 |
| Unit cell angles | 90.00, 90.16, 90.00 |
Refinement procedure
| Resolution | 41.900 - 2.990 |
| R-factor | 0.2359 |
| Rwork | 0.233 |
| R-free | 0.26550 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1wdn |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.893 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.170 |
| High resolution limit [Å] | 2.990 | 2.990 |
| Rmeas | 0.140 | 0.901 |
| Number of reflections | 61098 | 9748 |
| <I/σ(I)> | 8.86 | 1.52 |
| Completeness [%] | 99.6 | 98.8 |
| Redundancy | 3.79 | |
| CC(1/2) | 0.995 | 0.693 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 291.15 | 50 mM Tris (pH=7.5), 0.2 M Ammonium Sulfate, 30% PEG 4000 |
