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  • Title: Cloning, expression, purification, crystallization and preliminary X-ray crystallographic study of thymidylate kinase (TTHA1607) from Thermus thermophilus HB8.
    Author: Chaudhary SK, Jeyakanthan J, Sekar K.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2013 Feb 01; 69(Pt 2):118-21. PubMed ID: 23385749.
    Abstract:
    Nucleotide biosynthesis plays a key role in cell survival and cell proliferation. Thymidylate kinase is an enzyme that catalyses the conversion of dTMP to dTDP using ATP-Mg(2+) as a phosphoryl-donor group. This enzyme is present at the junction of the de novo and salvage pathways; thus, any inhibitor designed against it will result in cell death. This highlights the importance of this enzyme as a drug target. Thymidylate kinase from the extremely thermophilic organism Thermus thermophilus HB8 has been expressed, purified and crystallized using the microbatch method. The crystals diffracted to a resolution of 1.83 Å and belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 39.50, b = 80.29, c = 122.55 Å. Preliminary studies revealed the presence of a dimer in the asymmetric unit with a Matthews coefficient (V(M)) of 2.18 Å(3) Da(-1).
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