Abstract
A new crystal form of wild-type ribonucleotide reductase R2 from Escherichia coli was obtained. Crystals grow in space group P6122 with one R2 monomer in the asymmetric unit. A twofold crystallographic symmetry axis generates the physiological dimeric form of R2. Co-crystallization with CoCl2 or MnCl2 results in full occupancy of the dinuclear metal site. The structure of the MnII-loaded form was determined to 2.6 Å resolution by molecular replacement. The crystallization conditions, backbone conformation, crystal-packing interactions and metal centers are compared with those of previously determined crystal forms.
Original language | English (US) |
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Pages (from-to) | 1649-1654 |
Number of pages | 6 |
Journal | Acta Crystallographica Section D: Biological Crystallography |
Volume | 61 |
Issue number | 12 |
DOIs | |
State | Published - Dec 2005 |
ASJC Scopus subject areas
- Structural Biology
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Ribonucleotide Reductase R2 from Escherichia coli in space group P6(1)22
Sommerhalter, M. (Contributor), Saleh, L. (Contributor), Bollinger Jr., J. M. (Contributor) & Rosenzweig, A. C. (Contributor), Protein Data Bank (PDB), Nov 29 2005
DOI: 10.2210/pdb2ALX/pdb, https://www.wwpdb.org/pdb?id=pdb_00002alx
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