4JX9
Crystal structure of the complex of peptidyl t-RNA hydrolase from Acinetobacter baumannii with uridine at 1.4A 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 | 2012-11-20 |
Detector | MARRESEARCH |
Wavelength(s) | 0.97 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 33.945, 65.783, 75.752 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.040 - 1.400 |
R-factor | 0.1934 |
Rwork | 0.193 |
R-free | 0.20908 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4iko |
RMSD bond length | 0.004 |
RMSD bond angle | 1.118 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | AMoRE |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.040 | 1.430 |
High resolution limit [Å] | 1.400 | 1.400 |
Number of reflections | 32452 | |
Completeness [%] | 100.0 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 0.2M HEPES, 25% PEG400, 30% PEG1500, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |