It can supplement X ray-beam crystallography for investigations of small crystals (<0.1 micrometers), both inorganic, natural, and proteins, for example, layer proteins, that can't undoubtedly frame the substantial 3-dimensional precious stones required for that procedure. Protein structures are generally decided from either 2-dimensional gems (sheets or helices), polyhedrons, for example, viral capsids, or scattered individual proteins. Electrons can be utilized as a part of these circumstances, while X ray-beams can't, on account of electrons interface more emphatically with molecules than X-beams do. In this way, X-beams will go through a thin 2-dimensional precious stone without diffracting altogether, though electrons can be utilized to shape a picture.
On the other hand, the solid communication amongst electrons and protons makes thick gems impenetrable to electrons, which just enter short separations. One of the primary troubles in X ray-beam crystallography is deciding stages in the diffraction design. On account of the unpredictability of X-beam focal points, it is hard to frame a picture of the gem being diffracted, and subsequently stage data is lost. Luckily, electron magnifying instruments can resolve nuclear structure in genuine space and the crystallographic structure calculate stage data can be tentatively decided from a pictures Fourier change.