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1/2013
vol. 94 abstract:
Short communication
Inorganic pyrophosphatase (PPase) from a higher plant
Marta Grzechowiak
,
Michał Sikorski
,
Mariusz Jaskolski
BioTechnologia vol. 94(1) C pp. 35-37 C 2013
Online publish date: 2014/10/23
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Arabidopsis thaliana inorganic pyrophosphatase (AtPPA1) coding DNA (ppa1 gene) was cloned into bacterial expression
vector and overproduced in E. Coli cells as a His-tagged protein. The recombinant protein was purified from the bacterial lysate by two consecutive chromatographic steps: chelating chromatography on Ni2+-charged resin followed by FPLC size exclusion chromatography. The homogenous protein was submitted for crystallization. X-Ray diffraction data extending to 1.9Å resolution were collected using synchrotron radiation. The structure was solved by molecular replacement and refinement is in progress (R-factor below 20%). The structure of AtPP1 represents an alpha+beta protein fold which overlaps with other structural models for known bacterial and yeast inorganic pyrophosphatases. |