Cryogenic electron microscopy (cryo-EM) is a biophysical method to measure the structure of our protein of interest under very low temperatures (−183 °C or 90 K). The big advantage of this method is that protein crystals are not needed which means we can measure our proteins in a soluble but frozen state. After establishing a sufficient freezing protocol for our samples, the so-called grid-freezing, the native structure can be recorded. Having separate techniques of measuring protein structures allows the comparison of the structures in different environment, either in a crystal lattice or frozen in solution. This can give us more insights into the actual structure of our sample and eventual structural flexibilities depending on the environment.
To investigate our protein structures using cryo-EM, we are using the microscopes of the S2C2 center at SLAC.
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