Crystallization of human thymidylate synthase

J Mol Biol. 1991 May 20;219(2):161-3. doi: 10.1016/0022-2836(91)90558-n.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Cloning, Molecular
  • Crystallization
  • Escherichia coli / genetics
  • Humans
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Thymidylate Synthase / chemistry*
  • Thymidylate Synthase / genetics
  • Thymidylate Synthase / isolation & purification
  • X-Ray Diffraction / methods

Substances

  • Recombinant Proteins
  • Thymidylate Synthase