New Immunoglobulins Study Findings Reported from University of Texas (Single-step antibody-based affinity cryo-electron microscopy for imaging and structural analysis of macromolecular assemblies)
By a News Reporter-Staff News Editor at Life Science Weekly -- New research on Immunology is the subject of a report. According to news originating from San Antonio, Texas, by NewsRx correspondents, research stated, "Single particle cryo-electron microscopy (cryo-EM) is an emerging powerful tool for structural studies of macromolecular assemblies (i.e., protein complexes and viruses). Although single particle cryo-EM requires less concentrated and smaller amounts of samples than X-ray crystallography, it remains challenging to study specimens that are low-abundance, low-yield, or short-lived."
Our news journalists obtained a quote from the research from the University of Texas, "The recent development of affinity grid techniques can potentially further extend single particle cryo-EM to these challenging samples by combining sample purification and cryo-EM grid preparation into a single step. Here we report a new design of affinity cryo-EM approach, cryo-SPIEM, that applies a traditional pathogen diagnosis tool Solid Phase Immune Electron Microscopy (SPIEM) to the single particle cryo-EM method. This approach provides an alternative, largely simplified and easier to use affinity grid that directly works with most native macromolecular complexes with established antibodies, and enables cryo-EM studies of native samples directly from cell cultures. In the present work, we extensively tested the feasibility of cryo-SPIEM with multiple samples including those of high or low molecular weight, macromolecules with low or high symmetry, His-tagged or native particles, and high- or low-yield macromolecules."
According to the news editors, the research concluded: "Results for all these samples (non-purified His-tagged bacteriophage T7, His-tagged Escherichia coli ribosomes, native Sindbis virus, and purified but low-concentration native Tulane virus) demonstrated the capability of cryo-SPIEM approach in specifically trapping and concentrating target particles on TEM grids with minimal view constraints for cryo-EM imaging and determination of 3D structures."
For more information on this research see: Single-step antibody-based affinity cryo-electron microscopy for imaging and structural analysis of macromolecular assemblies. Journal of Structural Biology, 2014;187(1):1-9. Journal of Structural Biology can be contacted at: Academic Press Inc Elsevier Science, 525 B St, Ste 1900, San Diego, CA 92101-4495, USA. (Elsevier - www.elsevier.com; Journal of Structural Biology - www.elsevier.com/wps/product/cws_home/622900)
The news correspondents report that additional information may be obtained from G.M. Yu, Univ Texas Hlth Sci Center San Antonio, Dept. of Biochem, San Antonio, TX 78229, United States. Additional authors for this research include F. Vago, D.S. Zhang, J.E. Snyder, R. Yan, C. Zhang, C. Benjamin, X. Jiang, R.J. Kuhn, P. Serwer, D.H. Thompson and W. Jiang (see also Immunology).
Keywords for this news article include: Antibodies, Texas, Immunology, San Antonio, United States, Blood Proteins, Nanotechnology, Immunoglobulins, Emerging Technologies, North and Central America, Macromolecular Assemblies
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