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Improvement of the expression level, crystallization and preliminary X-ray diffraction studies of D-threo-3-hydroxyaspartate dehydratase isolated from Delftia sp. HT23 are reported.

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The glycine-rich loop of MK2 (MAPKAP-K2) bound to the non-selective inhibitor TEI-L03090 adopts the β-form, which is commonly found in other kinase complexes; however, it differs from the α-form which is adopted when MK2 is bound to the MK2-selective inhibitor TEI-I01800. These results show how conformational change of MK2 influences its selectivity.
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