Crystallization of human thymidylate synthase.
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.
Schiffer
C A
CA
Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.
Davisson
V J
VJ
Santi
D V
DV
Stroud
R M
RM
D003001:Cloning, Molecular; D003460:Crystallization; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D013940:Thymidylate Synthase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D014961:X-Ray Diffraction / Q000379:methods
D011994:Recombinant Proteins; D013940:Thymidylate Synthase