5EKT
Crystal structure of mutant-K146A of peptidyl-tRNA hydrolase from Vibrio cholerae at 1.63A resolution.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E+ SUPERBRIGHT |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2015-08-24 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.54 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 44.934, 74.295, 123.571 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.630 |
R-factor | 0.18914 |
Rwork | 0.187 |
R-free | 0.22810 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4zxp |
RMSD bond length | 0.018 |
RMSD bond angle | 1.970 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | HKL-2000 |
Refinement software | REFMAC (5.8.0131) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 1.630 |
Number of reflections | 46655 |
<I/σ(I)> | 32.1 |
Completeness [%] | 88.4 |
Redundancy | 5.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 296 | 100mM Sodium citrate (pH 8), 200mM Ammonium acetate, 20% PEG 4000 |