A major challenge of computational structural biology has been to create, from scratch, new proteins with heretofore unobserved three-dimensional structures. Researchers have now developed and demonstrated a methodology for protein-structure prediction and design by creating the first artificial globular protein with a novel topology. Significantly, the x-ray structure agreed almost precisely with the structure specified by the computational model. Read more »
ALS Work Using Protein Crystallography
Protein crystallography is used for determining the molecular structure of proteins. Crystallized protein molecules cause a beam of incident x-rays to scatter in many directions, with constructive and destructive interference generating a diffraction pattern. By analyzing these patterns, a crystallographer can produce a three-dimensional picture of the density of electrons within the crystal and thus determine the protein's structure.
The Path of Messenger RNA through the Ribosome
Using x-ray crystallography, researchers directly observed the path of mRNA in the 70S ribosome in Fourier difference maps at 7 Å resolution. Image depicts the view down the crystallographic 4-fold axis of the 70S ribosome-mRNA-tRNA complex, showing the head-to-tail juxtaposition of the model mRNAs (red-orange) between adjacent ribosomes. Read more »
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