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) |
|---|---|
| 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 |
All Science Journal Classification (ASJC) codes
- Structural Biology
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