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Purification, crystallization and preliminary X-ray analysis of uridine phosphorylase from Salmonella typhimurium by Mariya V. Dontsova; Yulia A. Savochkina; Azat G. Gabdoulkhakov; Sergey N. Baidakov; Andrey V. Lyashenko; Maria Zolotukhina; Liubov Errais Lopes; Mariya B. Garber; Ekaterina Yu. Morgunova; Stanislav V. Nikonov; Alexandr S. Mironov; Steven E. Ealick; Al'bert M. Mikhailov is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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The structural udp gene encoding uridine phosphorylase (UPh) was cloned from the Salmonella typhimurium chromosome and overexpressed in Escherichia coli cells. S. typhimurium UPh (StUPh) was puri®ed to apparent homogeneity and crystallized. The primary structure of StUPh has high homology to the UPh from E. coli, but the enzymes differ substantially in substrate speci®city and sensitivity to the polarity of the medium. Single crystals of StUPh were grown using hanging-drop vapor diffusion with PEG 8000 as the precipitant. X-ray diffraction data were collected to 2.9 A Ê resolution. Preliminary analysis of the diffraction data indicated that the crystal belonged to space group P6 1(5) , with unit-cell parameters a = 92.3, c = 267.5 A Ê . The solvent content is 37.7% assuming the presence of one StUPh hexamer per asymmetric unit.

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Author

Mariya V. Dontsova; Yulia A. Savochkina; Azat G. Gabdoulkhakov; Sergey N. Baidakov; Andrey V. Lyashenko; Maria Zolotukhina; Liubov Errais Lopes; Mariya B. Garber; Ekaterina Yu. Morgunova; Stanislav V. Nikonov; Alexandr S. Mironov; Steven E. Ealick; Al'bert M. Mikhailov

Publisher

International Union of Crystallography; Blackwell Publishing Inc.; International Union of Crystallography (IUCr) (ISSN 0907-4449)

Published

2004

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)