4FOT
Crystal structure of Peptidyl- tRNA Hydrolase from Acinetobacter baumannii at 2.20 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 | 34.550, 58.460, 109.250 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 51.540 - 2.200 |
| R-factor | 0.17293 |
| Rwork | 0.172 |
| R-free | 0.20066 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2pth |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.934 |
| 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] | 51.540 | 2.320 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.100 | 0.311 |
| Number of reflections | 11771 | |
| <I/σ(I)> | 13 | 3.7 |
| Completeness [%] | 99.3 | 95 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 0.2M HEPES buffer, 25% PEG10000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
