6A31
Crystal structure of Na+ bound Peptidyl-tRNA Hydrolase from Acinetobacter baumannii at 2.19 A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 300 |
| Detector technology | PIXEL |
| Collection date | 2018-05-13 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.9537 |
| Spacegroup name | P 21 2 21 |
| Unit cell lengths | 34.290, 58.750, 109.210 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 54.600 - 2.190 |
| R-factor | 0.17708 |
| Rwork | 0.174 |
| R-free | 0.23406 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4jy7 |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.732 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 54.600 | 2.230 |
| High resolution limit [Å] | 2.190 | 2.190 |
| Rmerge | 0.165 | 0.800 |
| Rmeas | 0.176 | 0.935 |
| Rpim | 0.058 | 0.301 |
| Number of reflections | 11810 | 11810 |
| <I/σ(I)> | 8.7 | 2.2 |
| Completeness [%] | 98.7 | 97 |
| Redundancy | 9.1 | 9.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 100 mM NaHEPES pH 7.5 25% PEG 1500 |
