Crystallization of human thymidylate synthase

UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology



Document Type


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.

Rights and Permissions

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

Related Resources

Link to Article in PubMed