2ALX : Ribonucleotide Reductase R2 from Escherichia coli in space group P6(1)22

  • Monika Sommerhalter (Contributor)
  • Lana Saleh (Contributor)
  • J. M. Bollinger (Contributor)
  • Amy C Rosenzweig (Contributor)

Dataset

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.
Date made available2005
PublisherRCSB-PDB

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