Preliminary X-ray diffraction studies of the putative catalytic domain of gamma delta resolvase from Escherichia coli.
Two crystal forms of the putative catalytic domain (residues 1-140) of gamma delta resolvase from Escherichia coli have been obtained. Type I is isomorphous with crystals of the intact protein, and type II is suitable for high resolution structure analysis. Type II crystals belong to the orthorhombic space group C222(1), with a = 76.8 A, b = 191.3 A, and c = 63.4 A. They contain two molecules (15,500 daltons each)/asymmetric unit and show diffraction beyond 2.7-A resolution. Calculation of a rotation function using 7-A data shows the orientation of the noncrystallographic axes.
D004926:Escherichia coli / Q000201:enzymology*; D009713:Nucleotidyltransferases; D019895:Transposases; D014961:X-Ray Diffraction
D009713:Nucleotidyltransferases; D019895:Transposases