title: Crystals of a catalytically defective, semisynthetic ribonuclease isomorphous with those of the fully active parent enzyme.
abstract: The enzymically active, semisynthetic, non-covalent complex formed by residues 1 through 118 and residues 111 through 124 of bovine pancreatic ribonuclease A crystallizes at pH 5.2 from (NH4)2SO4/CsCl solution with space group P3(2)21 and unit cell dimensions a and b = 67.7 A, c = 65.1 A and gamma = 120 degrees. The catalytically defective enzyme that results from the replacement of phenylalanine 120 by leucine crystallizes isomorphously with the parent structure (a and b = 67.2 A, c = 64.7 A, gamma = 120 degrees).
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003460:Crystallization; D004722:Endoribonucleases; D012259:Ribonuclease, Pancreatic
chemical_list: D004722:Endoribonucleases; D012259:Ribonuclease, Pancreatic