4FEX
Crystal structure of the aminoglycoside phosphotransferase APH(3')-Ia, with substrate kanamycin and small molecule inhibitor tyrphostin AG1478
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-02-18 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97856 |
| Spacegroup name | P 1 |
| Unit cell lengths | 57.669, 93.694, 96.318 |
| Unit cell angles | 118.84, 103.56, 93.44 |
Refinement procedure
| Resolution | 19.901 - 2.710 |
| R-factor | 0.1866 |
| Rwork | 0.184 |
| R-free | 0.24000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4ej7 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.304 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((phenix.refine: 1.7.3_928)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.760 |
| High resolution limit [Å] | 2.710 | 2.710 |
| Number of reflections | 45480 | |
| <I/σ(I)> | 19.39 | 2.043 |
| Completeness [%] | 98.9 | 98.5 |
| Redundancy | 3.9 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 2.5 | 298 | 0.1 M sodium acetate pH 4.5, 14% PEG3350, 0.3 M NDSB221, 2% DMSO, 2 mM kanamycin, 5 mM tyrphostin AG1478, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
