5YN4
Crystal structure of dimeric peptidyl tRNA hydrolase from Acinetobacter baumannii with occluded substrate binding site at 1.47 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 | 2017-07-05 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.966 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 34.556, 98.080, 123.812 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.590 - 1.470 |
R-factor | 0.17128 |
Rwork | 0.170 |
R-free | 0.20069 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5y98 |
RMSD bond length | 0.020 |
RMSD bond angle | 1.892 |
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] | 45.590 | 1.490 |
High resolution limit [Å] | 1.470 | 1.470 |
Rmerge | 0.136 | 0.605 |
Number of reflections | 55852 | 1978 |
<I/σ(I)> | 9.1 | 2.2 |
Completeness [%] | 98.4 | 92.4 |
Redundancy | 6.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 50mm HEPES, pH 7.5, PEG 1500 |