Abstract
X-ray diffraction at four temperatures from 220 to 300 K coupled with crystallographic refinement yields the mean-square displacements and conformational potentials of all 1,261 non-hydrogen atoms of metmyoglobin. The results are interpreted to indicate a condensed core around the haem, semi-liquid regions towards the outside and a possible pathway for ligands. It is concluded that X-ray diffraction can provide the spatial distribution of the dynamic features of a protein.
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Frauenfelder, H., Petsko, G. & Tsernoglou, D. Temperature-dependent X-ray diffraction as a probe of protein structural dynamics. Nature 280, 558–563 (1979). https://doi.org/10.1038/280558a0
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DOI: https://doi.org/10.1038/280558a0
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