Proceedings of the National Academy of Science (USA) published the research paper Atomic model of a cypovirus built from cryo on the 10th of January in the research institute of the Chinese Academy of Sciences Institute of Biophysics Zhu Ping, associate research fellow and others -EM structure provides insight into the mechanism of mRNA capping. The research was completed in collaboration with Zhu Ping and Sun Fei, the State Key Laboratory of Biomacromolecules, Institute of Biophysics, Sun Jingchen, Associate Professor of South China Agricultural University, and Zhang Jingqiang, Professor of Sun Yat-sen University. Among them, associate researcher Cheng Lingpeng of the Zhu Ping research group completed the work of cryo-electron microscopy imaging and structural analysis, assistant researcher Huang Xiaoxing assisted in the completion of virus purification work, and Zhang Kai, a graduate student in the research group of Sun Fei, assisted in the construction of the atomic model and the electron microscope platform of the Bioimaging Center Senior engineer Dr. Ji Gang provided technical support for electron microscope imaging.
In the second phase of the protein science research platform of the Chinese Academy of Sciences, the Institute of Biophysics of the Chinese Academy of Sciences focused on the development of a three-dimensional reconstruction research platform for biological macromolecular cryo-electron microscopy. It has built a world-leading bio-imaging technology laboratory with the most advanced 300 kV Titan Krios field emission cryo transmission electron microscope. The latest research is to use the cryo-electron microscope platform successfully debugged in April 2010 in the Bioimaging Technology Laboratory, and use single-particle image processing technology to obtain the near-atomic resolution three-dimensional structure of the plasmopolyhedrovirus of the Reoviridae family (3.9 Angstroms) ), And independently constructed an all-atom model.
This is the first analysis of the atomic structure model of biological macromolecules in China using cryo-electron microscopy technology, and the world's first all-atom model of a biomacromolecule complex obtained using CCD images of cryo-electron microscopy. This study confirmed the outflow channel of reovirus mRNA, localized two methyltransferases (7-N-methyltransferase and 2 "-O-methyltransferase) of reoviridae cytoplasmic polyhedrosis virus, and revealed How does the efflux channel guide mRNA through these two methyltransferases in order to complete the "capping" process. This finding is of great significance for studying the mechanism of dsRNA virus mRNA capping.
This result shows that the high-resolution research work of biological macromolecular cryo-electron microscopy independently carried out in China has reached the advanced level in this field. The research results and the series of results of the molecular chaperone structure published by Sun Fei's research group on the cover of Structure in October 2010 show that the successful establishment of the Bioimaging Technology Laboratory of the Protein Science Research Platform of the Chinese Academy of Sciences is aimed at further developing cryo-electron microscopy Cutting-edge research has laid a solid foundation.
This work was supported by projects such as the National Natural Science Foundation of the Fund Committee, the National Key Basic Research 973 Program of the Ministry of Science and Technology, and the Hundred Talents Program of the Chinese Academy of Sciences. Thesis link: http: //.
Scientists use cryo-electron microscopy for the first time to obtain an all-atom model of a biomacromolecule complex
Frozen electron microscopy image of cytoplasmic polyhedrosis virus CPV (upper left) and three-dimensional reconstruction of cytoplasmic polyhedrosis virus capsid (middle). The colored part of the reconstruction result is the most basic asymmetric structural unit that constitutes the virus. The image on the right shows an enlarged view of the asymmetric unit (top right) and the atomic model constructed (bottom right). The lower left figure shows the three-dimensional reconstructed electron density map of some amino acids and the constructed atomic model. The amino acid side chain can be clearly seen.
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