Protein degradation is a key mechanism for controlling a variety of cellular functions and pathways. One critical pathway, protein breakdown, is regulated by the 26S proteasome. As part of a cell’s central mechanism for protein degradation, the 26S proteasome could become a key molecular compound for cancer therapies. However, the instability of the 26S complex and its consequent dissociation into minor subcomplexes make it a difficult structure to elucidate.
Structural and computational biologists at the Max Planck Institute of Biochemistry have reconstructed the 26S and other key protein complexes in 3D from 2D projections obtained by cryo-electron microscopy. This work was made possible by the streamlined procedures for image acquisition, filtering, processing, and 3D reconstruction that the researchers developed using MathWorks tools.
"With MathWorks tools we can conduct the entire workflow in a single environment," says Andreas Korinek, scientist at the Max Planck Institute of Biochemistry. "Instead of converting coordinates and data between five or six different packages, we can use one platform for controlling instruments, acquiring and filtering images, and constructing 3D structures in an accelerated process."