Expression, purification and crystallization of MnSOD from Arabidopsis thaliana

Alexandra T. Marques, Sandra P. Santos, Margarida G. Rosa, Mafalda A A Rodrigues, Isabel Alexandra Aguiar de Abreu, Carlos Frazão, Célia V. Romão

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

Abstract

Manganese superoxide dismutase (MnSOD) is an essential primary antioxidant enzyme. MnSOD plays an important role in plant tolerance to abiotic stress and is a target candidate for increasing stress tolerance in crop plants. Although the structure and kinetic parameters of MnSODs from several organisms have been determined, this information is still lacking for plant MnSODs. Here, recombinant MnSOD from Arabidopsis thaliana (AtMnSOD) was expressed, purified and crystallized. A nearly complete data set could only be obtained when a total rotation range of 180° was imposed during data collection, despite the seemingly tetragonal metric of the AtMnSOD crystal diffraction. The data set extended to 1.95Å resolution and the crystal belonged to space group P1. Molecular-replacement calculations using an ensemble of homologous SOD structures as a search model gave a unique and unambiguous solution corresponding to eight molecules in the asymmetric unit. Structural and kinetic analysis of AtMnSOD is currently being undertaken.

Original languageEnglish
Pages (from-to)669-672
Number of pages4
JournalActa Crystallographica Section F:Structural Biology Communications
Volume70
Issue number5
DOIs
Publication statusPublished - 2014

Keywords

  • metalloproteins
  • oxidative stress
  • plants
  • ROS
  • SOD

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