9IVZ
Apg mutant enzyme D448A of acarbose hydrolase from human gut flora K. grimontii TD1, complex with acarbose
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 | 2023-12-16 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.97861 |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 75.480, 75.480, 400.802 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 37.740 - 2.290 |
| R-factor | 0.1885 |
| Rwork | 0.186 |
| R-free | 0.23050 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7vt9 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.991 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.740 | 2.370 |
| High resolution limit [Å] | 2.290 | 2.290 |
| Rmerge | 0.142 | 1.000 |
| Number of reflections | 31827 | 3044 |
| <I/σ(I)> | 10.9 | 2.2 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 6.6 | 6.9 |
| CC(1/2) | 0.997 | 0.865 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289.15 | 2.1 M DL-malic acid |
