Researchers from the Scripps Research Institute (TSRI) have provided what they claim is the first 3D visualization of the dynein-dynactin complex bound to microbubbles, which is responsible for cell division and preventing the development of neurological diseases. 

According to a recent press release from TSRI, researchers report that the dynactin protein connects two dyneins together to signal different molecules and organelles to different parts of the cell.  

"If you want a team of horses to move in one direction, you need to line them up," said lead author of the study Gabriel C. Lander, PhD, a TSRI associate professor. "That's exactly what dynactin is doing to dynein molecules." 

Lander and his colleagues specifically used cryo-electron tomography (similar to a CT scan of a protein) to produce the 3D reconstruction of the dynein-dynactin complex, according to the press release. Advance computational algorithms were them utilized to average out the numerous individual protein complexes resulting in a high-resolution image.  

"We're now able to move past cartoon models and visualize the fine details of many dynamic macromolecular complexes," concluded Danielle Grotjahn, a TSRI graduate student and co-author of the study. "As we learn more about the 3D organization and architecture of these molecular machines, we will be better equipped to understand how they malfunction in disease."