9DFC
Crystal structure of the wild-type Thermus thermophilus 70S ribosome in complex with lasso peptide lariocidin, mRNA, aminoacylated A-site Phe-tRNAphe, aminoacylated P-site fMet-tRNAmet, and deacylated E-site tRNAphe at 2.50A resolution
This is a non-PDB format compatible entry.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS-II BEAMLINE 17-ID-1 |
Synchrotron site | NSLS-II |
Beamline | 17-ID-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2024-03-15 |
Detector | DECTRIS EIGER X 9M |
Wavelength(s) | 1.033202 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 210.100, 451.030, 622.030 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.620 - 2.500 |
R-factor | 0.2185 |
Rwork | 0.216 |
R-free | 0.26530 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6xhw |
RMSD bond length | 0.008 |
RMSD bond angle | 1.387 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.8.2) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 48.620 | 48.620 | 2.560 |
High resolution limit [Å] | 2.500 | 11.180 | 2.500 |
Rmerge | 0.329 | 0.087 | 2.416 |
Rmeas | 0.342 | 0.091 | 2.515 |
Total number of observations | 27782616 | ||
Number of reflections | 2006670 | 23545 | 147863 |
<I/σ(I)> | 6.97 | 20.77 | 0.99 |
Completeness [%] | 100.0 | 99.5 | 100 |
Redundancy | 13.845 | 13.661 | 12.853 |
CC(1/2) | 0.989 | 0.993 | 0.185 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.6 | 292 | 0.1-0.2 M Arginine-HCl, 0.1M Tris-HCl pH 7.6, 2.5% PEG-20K, 7-12% MPD, 0.5 mM BME |