6IYE
Crystal structure of peptidyl-tRNA hydrolase from Acinetobacter baumannii with 12% PEG 1500 at 1.55 A 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 PILATUS 2M |
| Wavelength(s) | 0.96600 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 33.795, 65.849, 75.746 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 37.900 - 1.550 |
| R-factor | 0.25381 |
| Rwork | 0.253 |
| R-free | 0.27691 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5y9a |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.637 |
| 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] | 37.900 | 1.580 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.110 | 0.560 |
| Rmeas | 0.138 | 0.660 |
| Rpim | 0.068 | 0.330 |
| Number of reflections | 25090 | |
| <I/σ(I)> | 5.9 | 2.2 |
| Completeness [%] | 92.1 | |
| Redundancy | 3.78 | |
| CC(1/2) | 0.987 | 0.692 |
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 |
