J Mol Biol. 1991 May 20;219(2):161-3.

Crystallization of human thymidylate synthase.

Schiffer CA, Davisson VJ, Santi DV, Stroud RM.

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Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.

Abstract

Human thymidylate synthase has been crystallized in the absence of ligands and diffracts beyond 3.0 A. The protein was cloned and expressed in Escherichia coli and then crystallized from ammonium sulfate in the presence of beta-mercaptoethanol at a variety of pH values. The crystals are trigonal in the space-group P3(1)21; the unit cell dimensions are a = b = 96.7 A, c = 84.1 A.

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Replacement of Val3 in human thymidylate synthase affects its kinetic properties and intracellular stability . [Biochemistry. 2010]
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