A1 Refereed original research article in a scientific journal
Expression, purification and crystallization of Chaetomium thermophilum Cu,Zn superoxide dismutase
Authors: Wakadkar S, Zhang LQ, Li DC, Haikarainen T, Dhavala P, Papageorgiou AC
Publisher: WILEY-BLACKWELL PUBLISHING, INC
Publication year: 2010
Journal: Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Journal name in source: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS
Journal acronym: ACTA CRYSTALLOGR F
Volume: 66
First page : 1089
Last page: 1092
Number of pages: 4
ISSN: 1744-3091
DOI: https://doi.org/10.1107/S1744309110030393(external)
Abstract
Cu,Zn superoxide dismutase (Cu,ZnSOD) from the thermophilic fungus Chaetomium thermophilum was expressed in Pichia pastoris and purified. Crystals were grown in over 120 conditions but only those produced with 1.4 M sodium potassium phosphate pH 8.2 as precipitant were suitable for structural studies. Data were collected to 1.9 A resolution at 100 K from a single crystal using a synchrotron-radiation source. The crystals belonged to space group P6(1)/P6(5), with unit-cell parameters a = 90.2, c = 314.5 A and eight molecules in the asymmetric unit. Elucidation of the crystal structure will provide insights into the active site of the enzyme and a better understanding of the structure-activity relationship, assembly and thermal stability of Cu,ZnSODs.
Cu,Zn superoxide dismutase (Cu,ZnSOD) from the thermophilic fungus Chaetomium thermophilum was expressed in Pichia pastoris and purified. Crystals were grown in over 120 conditions but only those produced with 1.4 M sodium potassium phosphate pH 8.2 as precipitant were suitable for structural studies. Data were collected to 1.9 A resolution at 100 K from a single crystal using a synchrotron-radiation source. The crystals belonged to space group P6(1)/P6(5), with unit-cell parameters a = 90.2, c = 314.5 A and eight molecules in the asymmetric unit. Elucidation of the crystal structure will provide insights into the active site of the enzyme and a better understanding of the structure-activity relationship, assembly and thermal stability of Cu,ZnSODs.