Crystallization and preliminary crystallographic analysis of yeast cytosine deaminase.
Cytosine deaminase is an attractive candidate for anticancer gene therapy through its catalysis of the deamination of the prodrug 5-fluorocytosine to 5-fluorouracil. Recombinant yeast cytosine deaminase has been crystallized with the inhibitor 2-hydroxypyrimidine in 10% 2-propanol, 20% polyethylene glycol 4000, 0.1 M HEPES pH 7.5. The crystals belong to space group P2(1), with unit-cell parameters a = 45.31, b = 53.33, c = 64.29 A, beta = 99.98 degrees and one dimer per asymmetric unit. The crystals diffract X-rays beyond 1.5 A resolution and an initial atomic model has been built based on selenomethionyl multiwavelength anomalous data at 2 A resolution.
Hsu
Yi-Hsin
YH
Institute of Biopharmaceutical Science, National Yang-Ming University, Taipei, Taiwan.
Hu
Chih-Yung
CY
Lin
Jing-Jer
JJ
Liaw
Shwu-Huey
SH
D003460:Crystallization; D018360:Crystallography, X-Ray; D043525:Cytosine Deaminase / Q000737:chemistry*; D019281:Dimerization; D008958:Models, Molecular; D021122:Protein Subunits; D011994:Recombinant Proteins / Q000737:chemistry; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry; D012645:Selenomethionine / Q000737:chemistry
D021122:Protein Subunits; D011994:Recombinant Proteins; D029701:Saccharomyces cerevisiae Proteins; D012645:Selenomethionine; D043525:Cytosine Deaminase