CRYSTALLIZATION AND CRYSTALLOGRAPHIC INVESTIGATIONS OF THE SMALL-SUBUNIT OF MOUSE RIBONUCLEOTIDE REDUCTASE

The R2 protein component of mouse ribonucleotide reductase has been ob tained from overproducing Escherichia coli bacteria, It has been cryst allized using NaCl as precipitant, The crystals are orthorhombic, spac e group C222(1) with cell dimensions a = 76.9 Angstrom, b = 108.9 Angs trom, c = 92.7 Angstrom and diffract to at least 2.5 Angstrom. The asy mmetric unit of the crystals contains one monomer, Rotation and transl ation function searches using a model based on the weakly homologous E . coli R2 gave one significant peak, Rotation about a crystallographic 2-fold axis parallel to the a-axis produces an R2 dimer with dimer in teractions very similar to those found for E. coli R2.