8I4I
The asymmetric structure of homodimeric E. coli TrpRS bound with tryptophanyl adenylate and L-tryptophan
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 110 |
Detector technology | PIXEL |
Collection date | 2022-06-15 |
Detector | RIGAKU HyPix-6000HE |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 61.664, 80.048, 77.435 |
Unit cell angles | 90.00, 106.20, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.200 |
R-factor | 0.20797 |
Rwork | 0.207 |
R-free | 0.22900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5v0i |
RMSD bond length | 0.006 |
RMSD bond angle | 1.110 |
Data reduction software | CrysalisPro |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.320 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmeas | 0.131 | 0.556 |
Rpim | 0.055 | 0.278 |
Total number of observations | 20204 | |
Number of reflections | 36816 | 5332 |
<I/σ(I)> | 12.7 | 3.4 |
Completeness [%] | 99.9 | |
Redundancy | 5.4 | 3.8 |
CC(1/2) | 0.993 | 0.826 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 290 | 0.16M Ammonium sulfate, 0.1M HEPES pH 7.5, 25% PEG 3350 |