2alx
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Ribonucleotide Reductase R2 from Escherichia coli in space group P6(1)22
OverviewOverview
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.
About this StructureAbout this Structure
2ALX is a Single protein structure of sequence from Escherichia coli with MN and HG as ligands. Active as Ribonucleoside-diphosphate reductase, with EC number 1.17.4.1 Full crystallographic information is available from OCA.
ReferenceReference
Structure of Escherichia coli ribonucleotide reductase R2 in space group P6122., Sommerhalter M, Saleh L, Bollinger JM Jr, Rosenzweig AC, Acta Crystallogr D Biol Crystallogr. 2005 Dec;61(Pt 12):1649-54. Epub 2005, Nov 19. PMID:16301799
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