6MN4
Crystal structure of aminoglycoside acetyltransferase AAC(3)-IVa, H154A mutant, in complex with apramycin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-BM |
Synchrotron site | APS |
Beamline | 19-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-12-06 |
Detector | ADSC QUANTUM 210r |
Wavelength(s) | 0.97933 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 77.550, 130.507, 264.919 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.327 - 2.800 |
R-factor | 0.2487 |
Rwork | 0.247 |
R-free | 0.30430 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3sma |
RMSD bond length | 0.005 |
RMSD bond angle | 0.975 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHENIX |
Refinement software | PHENIX ((dev_3092: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.850 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.183 | 1.771 |
Rpim | 0.063 | 0.613 |
Number of reflections | 66374 | |
<I/σ(I)> | 12.77 | 1.4 |
Completeness [%] | 95.2 | 97.1 |
Redundancy | 9 | 8.9 |
CC(1/2) | 0.776 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 0.1 M HEPES pH 7, 30% (w/v) PEG1k, 2.5 mM apramycin |