Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.6
Classification:OXIDOREDUCTASE
Release Date:2005-11-29
Deposition Date:2005-08-08
Revision Date:2008-04-30#2011-07-13#2017-10-11
Molecular Weight:40548.18
Macromolecule Type:Protein
Residue Count:340
Atom Site Count:2788
DOI:10.2210/pdb2alx/pdb
Abstract:
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.
Resolution:2.6
Classification:OXIDOREDUCTASE
Release Date:2005-11-29
Deposition Date:2005-08-08
Revision Date:2008-04-30#2011-07-13#2017-10-11
Molecular Weight:40548.18
Macromolecule Type:Protein
Residue Count:340
Atom Site Count:2788
DOI:10.2210/pdb2alx/pdb
Abstract:
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.
| Date made available | 2005 |
|---|---|
| Publisher | RCSB-PDB |