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Crystallization and preliminary X-ray analysis of CYP153C1 from Novosphingobium aromaticivorans DSM12444 by Ruimin Zhou; Cong Huang; Aili Zhang; Stephen G. Bell; Weihong Zhou; Luet-Lok Wong is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Crystallization and preliminary X-ray analysis of CYP153C1 from Novosphingobium aromaticivorans DSM12444 about?

Cytochrome P450 (CYP) enzymes constitute a large family of haemoproteins that catalyze the monooxygenation of a great variety of endogenous and exogenous organic compounds. In common with other members of the CYP153 family of alkane hydroxylases, CYP153C1 from the oligotrophic bacterium Novosphingobium aromaticivorans DSM 12444 can bind linear alkanes such as heptane, octane and nonane. Here, the production, purification and crystallization of CYP153C1 and the collection of high-resolution diffraction data to 1.77 Å resolution are reported. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 61.0, b = 96.3, c = 149.8 Å, α = β = γ = 90.0°. Preliminary X-ray diffraction data analysis revealed that the asymmetric unit is most likely to contain two protein molecules.

Who reads Crystallization and preliminary X-ray analysis of CYP153C1 from Novosphingobium aromaticivorans DSM12444?

It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.

Author
Ruimin Zhou; Cong Huang; Aili Zhang; Stephen G. Bell; Weihong Zhou; Luet-Lok Wong
Publisher
John Wiley and Sons; International Union of Crystallography; John Wiley and Sons Ltd; International Union of Crystallography (IUCr) (ISSN 1744-3091)
Published
2011
Language
EN
Field
Biochemistry, Genetics and Molecular Biology (Life Sciences)

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