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Scytalone dehydratase Phe162Ala variant is a good target for investigating the substrate-binding mechanism of the enzyme. the variant enzyme was crystallized in its unligated state, and the diffraction data of the crystal were collected at 37 K using synchrotron X-rays.

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Crystallographic normal-mode refinement was carried out for the diffraction data of human lysozyme obtained at temperatures ranging from 113 to 178 K. The effects of a dynamic transition that occurred at about 150 K on the dynamic structures as well as the static structures of a protein molecule in a crystal are discussed.
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