9DFD
Crystal structure of the wild-type Thermus thermophilus 70S ribosome in complex with lasso peptide lariocidin B, mRNA, aminoacylated A-site Phe-tRNAphe, aminoacylated P-site fMet-tRNAmet, and deacylated E-site tRNAphe at 2.60A 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 | 2024-06-25 |
Detector | DECTRIS EIGER X 9M |
Wavelength(s) | 1.033210 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 210.290, 450.050, 626.340 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 365.480 - 2.600 |
R-factor | 0.2175 |
Rwork | 0.215 |
R-free | 0.26580 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6xhw |
RMSD bond length | 0.008 |
RMSD bond angle | 1.366 |
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] | 365.480 | 365.480 | 2.670 |
High resolution limit [Å] | 2.600 | 11.630 | 2.600 |
Rmerge | 0.263 | 0.039 | 2.140 |
Rmeas | 0.284 | 0.043 | 2.310 |
Total number of observations | 12513545 | ||
Number of reflections | 1791810 | 20946 | 130477 |
<I/σ(I)> | 7.44 | 29.67 | 0.95 |
Completeness [%] | 99.8 | 98.9 | 98.7 |
Redundancy | 6.984 | 6.801 | 6.943 |
CC(1/2) | 0.987 | 0.998 | 0.160 |
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 |