Crystallization and crystallographic data for new forms of thymidylate synthase from Lactobacillus casei.
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.
D003461:Crystallography; D007780:Lacticaseibacillus casei / Q000201:enzymology*; D011487:Protein Conformation; D013940:Thymidylate Synthase / Q000302:isolation & purification; D014961:X-Ray Diffraction
D013940:Thymidylate Synthase