Schiffer, Celia A.Davisson, V. JoSanti, Daniel V.Stroud, Robert M.2022-08-232022-08-231991-05-202010-02-05J Mol Biol. 1991 May 20;219(2):161-3.0022-2836 (Print)2038053https://hdl.handle.net/20.500.14038/25976Human 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.en-USCloning, MolecularCrystallizationEscherichia coliHumansProtein ConformationRecombinant ProteinsThymidylate SynthaseX-Ray DiffractionBiochemistry, Biophysics, and Structural BiologyPharmacology, Toxicology and Environmental HealthJournal Articlehttps://escholarship.umassmed.edu/bmp_pp/1041134077bmp_pp/104