5IVP
Crystal structure of the Peptidyl-tRNA hydrolase from Vibrio cholerae in the C121 space group at pH 6.5
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 | 2015-08-26 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.54 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 74.861, 44.507, 108.231 |
Unit cell angles | 90.00, 95.97, 90.00 |
Refinement procedure
Resolution | 107.640 - 2.010 |
R-factor | 0.1644 |
Rwork | 0.161 |
R-free | 0.22443 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4zxp |
RMSD bond length | 0.016 |
RMSD bond angle | 1.737 |
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] | 107.700 | 2.080 |
High resolution limit [Å] | 2.010 | 2.010 |
Number of reflections | 22748 | |
<I/σ(I)> | 32.5 | |
Completeness [%] | 95.7 | |
Redundancy | 6.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 288 | 0.1 M Sodium citrate 0.2 Ammonium acetate, 17.5 % Polyethylene glycol 4000 protein concentration 8 mg/ml |