4IKO
Structure of Peptidyl- tRNA Hydrolase from Acinetobacter baumannii at 1.90 A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 77 |
| Detector technology | CCD |
| Collection date | 2012-05-05 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.97 |
| Spacegroup name | P 21 2 21 |
| Unit cell lengths | 34.560, 58.220, 109.250 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 58.220 - 1.900 |
| R-factor | 0.16736 |
| Rwork | 0.156 |
| R-free | 0.19226 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2pth |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.822 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 58.220 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.100 | 0.537 |
| Number of reflections | 18051 | |
| <I/σ(I)> | 16.5 | 4.2 |
| Completeness [%] | 99.8 | 99.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 0.2M HEPES buffer, 25% PEG 10000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
