9IZO
Apg mutant enzyme D336A of acarbose hydrolase from human gut flora K. grimontii TD1, complex with acarviosine
This is a non-PDB format compatible entry.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL19U1 |
| Synchrotron site | SSRF |
| Beamline | BL19U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-01-19 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.97861 |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 75.510, 75.510, 399.409 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 46.650 - 2.130 |
| R-factor | 0.2106 |
| Rwork | 0.209 |
| R-free | 0.24790 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7vt9 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.959 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.660 | 2.190 |
| High resolution limit [Å] | 2.130 | 2.130 |
| Rmerge | 0.131 | 0.554 |
| Number of reflections | 39402 | 3126 |
| <I/σ(I)> | 6.8 | 2.1 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 6.1 | 6.1 |
| CC(1/2) | 0.991 | 0.887 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 289.15 | 0.1 M HEPES,PH 7.5 2.0 M Ammonium sulfate |
