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 |






