4FOP
Crystal Structure of Peptidyl-tRNA hydrolase from Acinetobacter baumannii at 1.86 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 | 2012-05-18 |
Detector | MARRESEARCH |
Wavelength(s) | 0.97 |
Spacegroup name | P 21 2 21 |
Unit cell lengths | 34.255, 57.864, 109.744 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 57.800 - 1.860 |
R-factor | 0.17785 |
Rwork | 0.175 |
R-free | 0.22795 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2pth |
RMSD bond length | 0.021 |
RMSD bond angle | 2.036 |
Data reduction software | AUTOMAR |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 57.800 | 1.930 |
High resolution limit [Å] | 1.860 | 1.860 |
Number of reflections | 17986 | |
<I/σ(I)> | 11.6 | 1.7 |
Completeness [%] | 99.1 | 99.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 310 | 0.2M HEPES Buffer, 25% PEG10000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 310K |