4GKI
Crystal structure of the aminoglycoside phosphotransferase APH(3')-Ia, with substrate kanamycin and small molecule inhibitor 1-NM-PP1
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 | 2012-04-22 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97856 |
| Spacegroup name | P 1 |
| Unit cell lengths | 96.843, 97.103, 112.128 |
| Unit cell angles | 103.24, 106.18, 112.66 |
Refinement procedure
| Resolution | 54.384 - 1.880 |
| R-factor | 0.1681 |
| Rwork | 0.166 |
| R-free | 0.21580 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4ej7 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.159 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((phenix.refine: 1.8_1069)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 99.630 | 1.980 |
| High resolution limit [Å] | 1.880 | 1.880 |
| Rmerge | 0.062 | 0.372 |
| Number of reflections | 265977 | |
| <I/σ(I)> | 7.6 | 2.1 |
| Completeness [%] | 97.6 | 96.5 |
| Redundancy | 2.3 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 298 | 0.1 M SODIUM ACETATE, 8% PEG3350, 3% DMSO, 2 MM KANAMYCIN, 3 mM 1-NM-PP1, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
