New 3D reconstruction method proposed to help determine protein structures

0 Comment(s)Print E-mail Xinhua, May 24, 2022
Adjust font size:

A joint research team has recently proposed a new 3D initial model reconstruction method to help study the protein structure in a more precise manner, according to Lanzhou University.

The method offers a new effective solution to obtain more precise initial models without references for single-particle analysis (SPA) in cryo-electron microscopy, said Lanzhou University.

The newly proposed method is of importance to the further study and the application research of biomedicine, said Lu Yonggang, a researcher at the School of Information Science and Engineering in Lanzhou University and the lead author of the research work.

SPA in cryo-electron microscopy has become a powerful tool for determining and studying the macromolecular structure at the atomic level. However, the existing methods may produce biased or even wrong final models. Situations become even worse when computing unsymmetrical initial models without references, according to Lu.

Researchers from China's Lanzhou University and Old Dominion University in the United States jointly carried out the research by using two spherical embeddings to determine the orientations of projection images, where the orientation is represented by the normal direction and the in-plane rotation of a projection image.

Compared to traditional methods, the new method has shown it is able to rectify the initial computation errors and produce a more accurate estimation of the projection angles, Lu said.

The study results have been published online in the journal Communications Biology.

Follow on Twitter and Facebook to join the conversation.
ChinaNews App Download
Print E-mail Bookmark and Share

Go to Forum >>0 Comment(s)

No comments.

Add your comments...

  • User Name Required
  • Your Comment
  • Enter the words you see:   
    Racist, abusive and off-topic comments may be removed by the moderator.
Send your storiesGet more from