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The crystal structures of thymidylate synthase (TS) supported a kink in beta-sheets which established the core of the enzyme. A mutant protein was prepared to examine the role of Gln214 in TS while in vitro site-directed mutagenesis was carried out to harvest derivatives of pTSO80 encoding mutations at location 214 of human TS. Results showed that increases in side chain volume at the 214 location significantly affected catalytic functions.