Crystallization and crystallographic data for new forms of thymidylate synthase from Lactobacillus casei

J Mol Biol. 1986 Sep 5;191(1):147-50. doi: 10.1016/0022-2836(86)90433-x.

Abstract

Several new crystal forms of thymidylate synthase (5,10-methlenetetrahydrofolate:dUMP C-methyltransferase; EC 2.1.1.45) were obtained by controlled pH change. In the crystals the dimeric molecule has a 2-fold symmetry axis coinciding with crystallographic symmetry. The crystals scatter to at least 2.7 A resolution in the synchrotron X-ray beam and appear to be suitable for high-resolution X-ray diffraction analysis. The crystals were successfully derivatized and preliminary results are reported for the covalent inhibitory ternary complex of thymidylate synthase, 5-fluoro-2'-deoxyuridylate and 5,10-methylenetetrahydrofolate.

Publication types

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

MeSH terms

  • Crystallography
  • Lacticaseibacillus casei / enzymology*
  • Protein Conformation
  • Thymidylate Synthase* / isolation & purification
  • X-Ray Diffraction

Substances

  • Thymidylate Synthase