5YN4
Crystal structure of dimeric peptidyl tRNA hydrolase from Acinetobacter baumannii with occluded substrate binding site at 1.47 A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-07-05 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.966 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 34.556, 98.080, 123.812 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.590 - 1.470 |
| R-factor | 0.17128 |
| Rwork | 0.170 |
| R-free | 0.20069 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5y98 |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.892 |
| Data reduction software | XDS |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.590 | 1.490 |
| High resolution limit [Å] | 1.470 | 1.470 |
| Rmerge | 0.136 | 0.605 |
| Number of reflections | 55852 | 1978 |
| <I/σ(I)> | 9.1 | 2.2 |
| Completeness [%] | 98.4 | 92.4 |
| Redundancy | 6.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 50mm HEPES, pH 7.5, PEG 1500 |
