A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Expression, purification and crystallization of Chaetomium thermophilum Cu,Zn superoxide dismutase
Tekijät: Wakadkar S, Zhang LQ, Li DC, Haikarainen T, Dhavala P, Papageorgiou AC
Kustantaja: WILEY-BLACKWELL PUBLISHING, INC
Julkaisuvuosi: 2010
Journal: Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Tietokannassa oleva lehden nimi: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS
Lehden akronyymi: ACTA CRYSTALLOGR F
Vuosikerta: 66
Aloitussivu: 1089
Lopetussivu: 1092
Sivujen määrä: 4
ISSN: 1744-3091
DOI: https://doi.org/10.1107/S1744309110030393
Tiivistelmä
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.
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