Why care about cryo-EM?
The function of vast majority of proteins is critically dependent on their three-dimensional structure. Therefore, in order to really understand how the proteins function, we must know their structure at atomic level. For a long time, x-ray crystallography and nuclear magnetic resonance (NMR) were methods of choice for almost all obtained atomic resolution structures of proteins. The third method is cryo-electron microscopy (cryo-EM). This does not require crystals or labels and often proteins can be studied very close to physiological conditions. Although cryo-EM still suffers from a number of limitations, it is clearly a rapidly developing technique and in future might become method of choice for structure determination of most biomolecules.
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Why care about cryo-EM?
The function of vast majority of proteins is critically dependent on their three-dimensional structure. Therefore, in order to really understand how the proteins function, we must know their structure at atomic level. For a long time, x-ray crystallography and nuclear magnetic resonance (NMR) were methods of choice for almost all obtained atomic resolution structures of proteins. The third method is cryo-electron microscopy (cryo-EM). This does not require crystals or labels and often proteins can be studied very close to physiological conditions. Although cryo-EM still suffers from a number of limitations, it is clearly a rapidly developing technique and in future might become method of choice for structure determination of most biomolecules.
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