8TDF
Structure of Alistipes sp. Glucoside-3-dehydrogenase AL3
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08ID-1 |
| Synchrotron site | CLSI |
| Beamline | 08ID-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-08-11 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.9537 |
| Spacegroup name | I 1 2 1 |
| Unit cell lengths | 180.635, 56.751, 220.447 |
| Unit cell angles | 90.00, 108.87, 90.00 |
Refinement procedure
| Resolution | 48.000 - 2.100 |
| R-factor | 0.20027 |
| Rwork | 0.198 |
| R-free | 0.23265 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.015 |
| RMSD bond angle | 2.065 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0415) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.000 | 2.140 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.174 | 1.619 |
| Rmeas | 0.189 | 1.750 |
| Rpim | 0.073 | 0.659 |
| Total number of observations | 822967 | 41507 |
| Number of reflections | 123819 | 6021 |
| <I/σ(I)> | 7.2 | 1.5 |
| Completeness [%] | 99.7 | |
| Redundancy | 6.6 | 6.9 |
| CC(1/2) | 0.994 | 0.513 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.15 M Sodium Malonate 19% PEG 3350 |
