5YL8
The crystal structure of inactive dimeric peptidyl-tRNA hydrolase from Acinetobacter baumannii at 1.79 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 | CCD |
Collection date | 2017-09-17 |
Detector | MARRESEARCH |
Wavelength(s) | 0.9724 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 34.530, 98.490, 123.090 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 76.900 - 1.790 |
R-factor | 0.1767 |
Rwork | 0.175 |
R-free | 0.20840 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5y98 |
RMSD bond length | 0.020 |
RMSD bond angle | 2.087 |
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] | 76.900 | 1.818 |
High resolution limit [Å] | 1.790 | 1.790 |
Rmerge | 0.067 | 0.622 |
Number of reflections | 37544 | 1911 |
<I/σ(I)> | 13.1 | |
Completeness [%] | 92.0 | 94.3 |
Redundancy | 4.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 50mM Na HEPES, PEG 1500 |