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 |