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|Title:||Purification, crystallization and preliminary X-ray analysis of cytochrome P450 219A1 from Novosphingobium aromaticivorans DSM 12444|
|Citation:||Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, 2009; 65(4):364-367|
|Chuan Hong, Stephen G. Bell, Wen Yang, Hui Wang, Yiming Hao, Xin Li, Weihong Zhou, Mark Bartlam, and Luet-Lok Wong|
|Abstract:||Cytochrome P450 enzymes catalyze a variety of reactions and are widely distributed in living organisms. In recent studies, the first members of five new families of cytochrome P450 enzymes have been identified, including cytochrome P450 219A1 (CYP219A1) from Novosphingobium aromaticivorans DSM 12444. It has also been reported that isolongifolen-9-one (C15H22O), a sesquiterpenoid ketone derivative, is a potential substrate for CYP219A1, inducing a [greater-than or equal to]95% shift of the haem spin state to high spin upon binding. The CYP219A1 protein has been crystallized and single crystals have been studied by X-ray crystallography. Diffraction data were collected to 2.4 Å resolution. The crystals belonged to space group P6, with unit-cell parameters a = 93.1, b = 93.1, c = 98.0 Å. Preliminary X-ray diffraction data analysis revealed that the asymmetric unit contained one protein molecule.|
|Keywords:||cytochrome P450 219A1; Novosphingobium aromaticivorans DSM 12444|
|Rights:||© 2009 International Union of Crystallography|
|Appears in Collections:||Chemistry and Physics publications|
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