Crystallization and crystallographic investigations of the small subunit of mouse ribonucleotide reductase.
The R2 protein component of mouse ribonucleotide reductase has been obtained from overproducing Escherichia coli bacteria. It has been crystallized using NaCl as precipitant. The crystals are orthorhombic, space group C222(1), with cell dimensions a = 76.9 A, b = 108.9 A, c = 92.7 A and diffract to at least 2.5 A. The asymmetric unit of the crystals contains one monomer. Rotation and translation 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 interactions very similar to those found for E. coli R2.
Nielsen
B B
BB
Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala, Sweden.
Kauppi
B
B
Thelander
M
M
Thelander
L
L
Larsen
I K
IK
Eklund
H
H
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D005583:Fourier Analysis; D007501:Iron / Q000032:analysis; D051379:Mice; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D012264:Ribonucleotide Reductases / Q000737:chemistry*
D011994:Recombinant Proteins; D007501:Iron; D012264:Ribonucleotide Reductases