Crystal diffraction3/30/2023 ![]() Resolution", that is, the disorder it too great to permitĭetermination of molecular structure. More than half of theĬrystals obtained from various purified proteins are not of "atomic Of the available crystals determines resolution. Length of X-rays (on the order of 1 Å), but in practice, the quality Resolution is theoretically limited by the wave In crystals of macromolecules, it is the degree of order in theĬrystal ("quality of the crystal") that limits the resolution of X-rayĬrystallography. I googled to find a more elaborate explanation the closest thing I found was on Proteopedia, but it actually repeats the same: what defines the resolution limit), if that is even possible.Īs you wrote in the question, the diffraction limit of the crystal is often explained by saying "it was not well ordered". I am not that strong in math/physics and find the general information on resolution limits (Braggs limit) to be very convoluted, and would therefore appreciate an intuitive explanation of how this works (i.e. ![]() I assume this is somehow explained when I understand what defines the resolution limit (?). I am assume that it has something to do with Braggs law and the Ewald sphere construction? I am also not completely sure why the outer diffraction spots represents the higher resolution and the inner spots represents the lower resolution. 1.5Å with more technical (specific) terms other than "it was not well ordered". However, imagine that you collect a dataset (diffraction images) from a protein crystal and notice that the outer spots are located at a resolution of about 2.2Å, how can you explain that this crystal did not diffract to e.g. arrangement of the macromolecules) in a protein crystal determines how well it diffracts when hit by an x-ray beam. I understand that the inner symmetry (i.e. My question regards diffraction patterns and resolution limit of protein crystals.
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