Crystallization and preliminary X-ray diffraction analysis of cytotoxic ribonucleases from bullfrog Rana catesbeiana.
RC-RNases are ribonucleases from Rana catesbeiana oocytes with pyrimidine-guanine sequence specificity. They also possess cell cytotoxicity and lectin activity. Protein crystals of three RC-RNase isozymes, RC-RNase 3, RC-RNase 4 and RC-RNase 6, were grown in various crystal systems under different conditions. Crystals of RC-RNase3 belong to the orthorhombic C222(1) space group, with unit-cell parameters a = 66.66, b = 97.38, c = 85.74 A. Crystals of RC-RNase 4 belong to the trigonal space group P3(1) or P3(2), with unit-cell parameters a = b = 32.22, c = 92.12 A. Crystals of RC-RNase 6 complexed with cytidylyl 2'-5' guanosine belong to the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 61.80, c = 65.96 A.
Liu
J H
JH
Department of Life Science, National Tsing Hua University, Hsinchu 300, Taiwan.
Liao
Y D
YD
Sun
Y J
YJ
D029845:Amphibian Proteins; D000818:Animals; D001798:Blood Proteins / Q000737:chemistry; D003460:Crystallization; D018360:Crystallography, X-Ray; D004722:Endoribonucleases / Q000737:chemistry*; D047091:Eosinophil Granule Proteins; D011487:Protein Conformation; D011892:Rana catesbeiana / Q000378:metabolism*; D012260:Ribonucleases
D029845:Amphibian Proteins; D001798:Blood Proteins; D047091:Eosinophil Granule Proteins; D004722:Endoribonucleases; D012260:Ribonucleases; C031956:2-5A-dependent ribonuclease; C094067:pyrimidine-guanine sequence-specific ribonuclease, Rana catesbeiana