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Research article - Peer-reviewed, 2003

Expression and preliminary crystallographic studies of R1E, the large subunit of ribonucleotide reductase from Salmonella typhimurium

Uppsten M, Farnegardh M, Jordan A, Ramaswamy S, Uhlin U


The nrdE gene product R1E, the large subunit of the class 1b Salmonella typhimurium ribonucleotide reductase, has been overexpressed, purified and crystallized. Initially, the protein crystallized in two orthorhombic space groups, C222(1) and P2(1)2(1)2, using tartrate and PEG 6000 as precipitants, respectively Better diffracting crystals belonging to the tetrahedral space group P4(3)2(1)2 were obtained using sodium malonate as precipitant. The P4(3)2(1)2 crystals could only be obtained after seeding from a drop containing C222(1) crystals grown in sodium tartrate. Thus, streak-seeding resulted in crystals of a supergroup to C222(1). Data to 2.8 Angstrom resolution have been collected on the P4(3)2(1)2 crystals which contained one R1E subunit in the asymmetric unit


ribonucleotide reductase (RNR); nrdE; catalytic subunit; seeding

Published in

Acta Crystallographica Section D: Biological Crystallography
2003, Volume: 59, pages: 1081-1083

    SLU Authors

    • Uhlin, Ulla

      • Department of Molecular Biology, Swedish University of Agricultural Sciences
      • Uppsten, Malin

        • Department of Molecular Biology, Swedish University of Agricultural Sciences

      UKÄ Subject classification

      Veterinary Science
      Animal and Dairy Science
      Agricultural Science

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