26WD
Structure of honeybee alpha-amylase belonging to glycoside hydrolase family 13 subfamily 15
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL45XU |
| Synchrotron site | SPring-8 |
| Beamline | BL45XU |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-10-05 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 89.729, 89.729, 122.193 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 44.860 - 1.900 |
| R-factor | 0.2044 |
| Rwork | 0.203 |
| R-free | 0.22970 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | AlphaFold |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.625 |
| 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 | 2.010 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Number of reflections | 40052 | 6355 |
| <I/σ(I)> | 13.7 | |
| Completeness [%] | 99.8 | |
| Redundancy | 52.8 | |
| CC(1/2) | 0.997 | 0.586 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 10 mM acarbose, 0.1 M imidazole-HCl (pH 8.0), 40% PEG400 |
