8TDH
Structure of trehalose bound Alistipes sp. Glucoside-3-dehydrogenase AL3
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-03-11 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 1.0332 |
| Spacegroup name | I 1 2 1 |
| Unit cell lengths | 186.581, 57.221, 224.962 |
| Unit cell angles | 90.00, 106.58, 90.00 |
Refinement procedure
| Resolution | 162.267 - 2.950 |
| Rwork | 0.195 |
| R-free | 0.24710 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 5.641 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0425) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 162.270 | 3.060 |
| High resolution limit [Å] | 2.950 | 2.950 |
| Rmerge | 0.141 | 0.462 |
| Rmeas | 0.199 | 0.654 |
| Rpim | 0.141 | 0.462 |
| Number of reflections | 43707 | 3079 |
| <I/σ(I)> | 3.5 | |
| Completeness [%] | 89.9 | |
| Redundancy | 2.7 | 1.9 |
| CC(1/2) | 0.950 | 0.497 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.25 M Sodium Malonate 17% PEG 3350 |
