5GVZ
Crystal structure of Peptidyl-tRNA hydrolase from Vibrio cholerae in space group C2221 at resolution 1.75A.
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 | 2016-03-10 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.5418 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 46.136, 73.462, 120.520 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.750 |
R-factor | 0.1932 |
Rwork | 0.191 |
R-free | 0.23499 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4zxp |
RMSD bond length | 0.019 |
RMSD bond angle | 1.897 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.810 |
High resolution limit [Å] | 1.750 | 1.750 |
Number of reflections | 20981 | |
<I/σ(I)> | 50.1 | |
Completeness [%] | 99.3 | |
Redundancy | 12.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 293 | 100 mM sodium acetate (pH 5.6), 200 mM potassium sodium tartrate, 2M Ammonium sulfate |