5F49
Crystal structure of an aminoglycoside acetyltransferase meta-AAC0020 from an uncultured soil metagenomic sample in complex with malonyl-coenzyme A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 HF |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2015-07-15 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 |
| Unit cell lengths | 46.159, 54.047, 84.847 |
| Unit cell angles | 72.30, 74.57, 88.07 |
Refinement procedure
| Resolution | 23.487 - 2.150 |
| R-factor | 0.1939 |
| Rwork | 0.192 |
| R-free | 0.22660 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | apoenzyme |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.929 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.190 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmerge | 0.093 | 0.577 |
| Number of reflections | 39176 | |
| <I/σ(I)> | 16.96 | |
| Completeness [%] | 95.6 | 92.9 |
| Redundancy | 2.6 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 298 | 18% PEG 8000, 0.2 M calcium acetate hydrate, 0.1 M sodium cacodylate |
