6IVV
Structure of peptidyl-tRNA hydrolase from Acinetobacter baumannii with multiple surface binding regions at 1.26A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-1 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-11-08 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 0.96600 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 33.945, 66.034, 75.711 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.770 - 1.260 |
| R-factor | 0.15901 |
| Rwork | 0.158 |
| R-free | 0.18422 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5y9a |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.936 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.770 | 1.340 |
| High resolution limit [Å] | 1.260 | 1.260 |
| Rmerge | 0.060 | 0.800 |
| Rmeas | 0.077 | |
| Number of reflections | 46366 | |
| <I/σ(I)> | 8.42 | |
| Completeness [%] | 97.2 | |
| Redundancy | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 12% PEG 1500, 0.1M HEPES PH 7.5 |
