Crystallization of human thymidylate synthase
Department of Biochemistry and Molecular Pharmacology
Cloning, Molecular; Crystallization; Escherichia coli; Humans; Protein Conformation; Recombinant Proteins; Thymidylate Synthase; X-Ray Diffraction
Biochemistry, Biophysics, and Structural Biology | Pharmacology, Toxicology and Environmental Health
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.
J Mol Biol. 1991 May 20;219(2):161-3.
Journal of molecular biology
Schiffer CA, Davisson V, Santi DV, Stroud RM. (1991). Crystallization of human thymidylate synthase. Biochemistry and Molecular Biotechnology Publications. Retrieved from https://escholarship.umassmed.edu/bmp_pp/104