6BFF
Structure of the aminoglycoside acetyltransferase AAC(6')-Im
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL12-2 |
| Synchrotron site | SSRL |
| Beamline | BL12-2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2012-01-13 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.9795 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 161.550, 34.950, 67.320 |
| Unit cell angles | 90.00, 102.33, 90.00 |
Refinement procedure
| Resolution | 34.123 - 1.700 |
| R-factor | 0.1868 |
| Rwork | 0.185 |
| R-free | 0.22930 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4qc6 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.931 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.600 | 1.750 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.061 | 0.577 |
| Number of reflections | 39826 | 2771 |
| <I/σ(I)> | 12.9 | 2.3 |
| Completeness [%] | 96.9 | 91.8 |
| Redundancy | 3.6 | 3.5 |
| CC(1/2) | 0.998 | 0.784 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 277 | 0.2 M MgCl2, 0.1 M Tris HCl pH 8.5, 30% PEG 4000 |
