Structure of Escherichia coli ribonucleotide reductase R2 in space group P6122.
A new crystal form of wild-type ribonucleotide reductase R2 from Escherichia coli was obtained. Crystals grow in space group P6(1)22 with one R2 monomer in the asymmetric unit. A twofold crystallographic symmetry axis generates the physiological dimeric form of R2. Co-crystallization with CoCl(2) or MnCl(2) results in full occupancy of the dinuclear metal site. The structure of the Mn(II)-loaded form was determined to 2.6 Angstroms resolution by molecular replacement. The crystallization conditions, backbone conformation, crystal-packing interactions and metal centers are compared with those of previously determined crystal forms.
Sommerhalter
Monika
M
Department of Biochemistry, Northwestern University, Evanston, IL 60208, USA.
Saleh
Lana
L
Bollinger
J Martin
JM
Rosenzweig
Amy C
AC
D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology; D008958:Models, Molecular; D011487:Protein Conformation; D012264:Ribonucleotide Reductases / Q000737:chemistry*
D012264:Ribonucleotide Reductases; C108427:ribonucleotide reductase R2 subunit