Expression, purification and crystallization of MnSOD from Arabidopsis thaliana. Issue 5 (1st May 2014)

• Record Type: Journal Article
• Authors: Marques, Alexandra T.; Santos, Sandra P.; Rosa, Margarida G.; Rodrigues, Mafalda A. A.; Abreu, Isabel A.; Frazão, Carlos; Romão, Célia V.
• Is Part Of: Acta crystallographica. Volume 70:Issue 5(2014:May)
• Page Start: 669
• Page End: 672
• Publication Date: 2014-05-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X14007687
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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 <italic>Arabidopsis thaliana</italic> (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 1.95 Å resolution and the crystal belonged to space group <italic>P</italic>1. 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.</p> </abstract>