5ZZV
Crystal structure of PEG-1500 crystallized Peptidyl-tRNA Hydrolase from Acinetobacter baumannii at 1.5 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 | 2018-05-13 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 0.9095 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 109.025, 34.383, 58.659 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.930 - 1.570 |
R-factor | 0.17177 |
Rwork | 0.170 |
R-free | 0.20544 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4fop |
RMSD bond length | 0.019 |
RMSD bond angle | 1.888 |
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] | 39.930 | 1.630 |
High resolution limit [Å] | 1.570 | 1.570 |
Rmeas | 0.145 | 0.145 |
Number of reflections | 24836 | 24836 |
<I/σ(I)> | 8.7 | 8.7 |
Completeness [%] | 99.5 | 99.5 |
Redundancy | 12 | 12 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 100mM HEPES, 15% PEG 1500 |