7Y52
Crystal structure of peptidyl-tRNA hydrolase from Enterococcus faecium
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 | 2022-03-29 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.54178 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 38.821, 74.835, 63.751 |
Unit cell angles | 90.00, 104.85, 90.00 |
Refinement procedure
Resolution | 23.780 - 1.920 |
R-factor | 0.1865 |
Rwork | 0.184 |
R-free | 0.23390 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4yly |
RMSD bond length | 0.013 |
RMSD bond angle | 1.278 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 35.000 | 35.000 | 1.990 |
High resolution limit [Å] | 1.920 | 4.130 | 1.920 |
Rmerge | 0.057 | 0.033 | 0.292 |
Rmeas | 0.061 | 0.036 | 0.316 |
Rpim | 0.023 | 0.013 | 0.118 |
Total number of observations | 193162 | ||
Number of reflections | 26521 | 2710 | 2617 |
<I/σ(I)> | 15.4 | ||
Completeness [%] | 100.0 | 99.6 | 100 |
Redundancy | 7.3 | 7.4 | 7.1 |
CC(1/2) | 0.999 | 0.968 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 295 | 0.2 M Ammonium Sulfate, 0.1 M Tris-HCl pH 7.5, 15% PEG 4K |