24IR
alpha-1,2-glucosidase from Arthrobacter humicola A8F5
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-1A |
| Synchrotron site | Photon Factory |
| Beamline | BL-1A |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2025-05-18 |
| Detector | DECTRIS EIGER X 4M |
| Wavelength(s) | 1.007 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 55.882, 109.943, 105.234 |
| Unit cell angles | 90.00, 93.66, 90.00 |
Refinement procedure
| Resolution | 47.430 - 1.880 |
| R-factor | 0.20943 |
| Rwork | 0.207 |
| R-free | 0.25715 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | AlphaFold |
| RMSD bond length | 0.015 |
| RMSD bond angle | 2.454 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0425) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.700 | 1.910 |
| High resolution limit [Å] | 1.880 | 1.880 |
| Rmerge | 0.175 | 0.928 |
| Rmeas | 0.207 | 1.092 |
| Number of reflections | 103014 | 5090 |
| <I/σ(I)> | 5 | 1.5 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 3.5 | 3.6 |
| CC(1/2) | 0.977 | 0.536 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.8 | 293 | 0.1 M sodium acetate pH5.1 , 34%(v/v)1,2-propanediol |
