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 |
