Cryo-Electron Microscopy (Cryo-EM) is a structural biology technique that utilizes high-speed electrons as a source beam to acquire structural insights into the studied biological system. Typically, the biological sample is rapidly frozen in vitreous ice. Subsequently, the cryo sample is examined and imaged in an electron microscope while maintained at liquid nitrogen temperatures.
The 2017 Nobel Prize in Chemistry was granted to three researchers for their advancements in cryo-electron microscopy, a technique enabling high-resolution structure determination of biomolecules in solution. The laureates include Jacques Dubochet from the University of Lausanne, Switzerland; Joachim Frank from Columbia University, New York, US; and Richard Henderson from the Medical Research Council Laboratory of Molecular Biology in Cambridge, UK. Their collective contributions have facilitated the visualization of intricate structures of proteins, nucleic acids, and other biomolecules, allowing scientists to observe their movements and changes during functional activities.
To enhance accessibility to advanced cryo-electron microscopy (cryo-EM) microscopes, the National Institutes of Health (NIH) has established three national centers where researchers lacking access can submit their samples for analysis. However, the hub-and-spokes system faces challenges. Rajan frequently experiences delays of several months in obtaining results from the national centers, only to discover that her samples were ineffective. Despite improving her protein freezing techniques, Rajan estimates that fewer than 10% of her samples have yielded satisfactory data.
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