Cryo-electron microscopy (Cryo-EM) is a microscopy technique that uses electrons to image frozen biological specimens at the molecular level. It offers a unique way to visualize the structures of macromolecules and their complexes such as viruses, proteins and DNA that are too small to be seen with an optical microscope. The technique has revolutionized the way researchers can study proteins and other molecular structures. Cryo-EM works by rapidly freezing a sample in an ultralow temperature environment, which preserves the sample in its native form and prevents any damage that can be caused by traditional electron microscopy. The sample is then placed in a vacuum chamber and bombarded with electrons, which are then scattered off the sample. These scattered electrons are then detected by a detector, which creates a three-dimensional image of the sample. It is then possible to reconstruct the structure of the molecules in the sample. Cryo-EM has many advantages over traditional electron microscopy. It allows for the visualization of a sample in its native state, without the need for specimen preparation. This reduces the amount of time and resources required to image a sample. Additionally, the resolution of the image produced is much higher than that of traditional electron microscopy, allowing researchers to observe the structures of proteins and other molecules at an unprecedented level of detail. Cryo-EM is being used in many different fields, such as structural biology, biochemistry, and pharmaceutical research. It is being used to study the structure of proteins, viruses, and other macromolecules, as well as to gain insights into the function of these molecules.
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