title: Crystallization and preliminary crystallographic data of ribonucleotide reductase protein B2 from Escherichia coli.
abstract: The B2 subunit of ribonucleotide reductase from Escherichia coli has been crystallized from ammonium sulfate solutions at pH 6.0. Crystals grew as orthorhombic plates with cell dimensions a = 58 A, b = 73 A, and c = 205 A. The asymmetric unit probably contains one B2 dimer of molecular weight 2 X 43,000. The packing of molecules in the crystals is compatible with an elongated shape of the dimer. The crystals diffract to 2.5 A and are suitable for structural work.
mesh_terms: D004926:Escherichia coli / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D011487:Protein Conformation; D012264:Ribonucleotide Reductases / Q000302:isolation & purification*; D014961:X-Ray Diffraction
chemical_list: D046911:Macromolecular Substances; D012264:Ribonucleotide Reductases