Crystallization of human thymidylate synthase
Department of Biochemistry and Molecular Pharmacology
Medical Subject Headings
Cloning, Molecular; Crystallization; Escherichia coli; Humans; Protein Conformation; Recombinant Proteins; Thymidylate Synthase; X-Ray Diffraction
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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Citation: J Mol Biol. 1991 May 20;219(2):161-3.
Schiffer, Celia A.; Davisson, V. Jo; Santi, Daniel V.; and Stroud, Robert M., "Crystallization of human thymidylate synthase" (1991). Biochemistry and Molecular Pharmacology Publications and Presentations. Paper 104.