Inorganic pyrophosphatase (PPase)
from a higher plant

Grzechowiak M, Sikorski M, Jaskolski M. Inorganic pyrophosphatase (PPase)
from a higher plant. BioTechnologia. 2014;94(1):35-37. doi:10.5114/bta.2013.46433.

APA

Grzechowiak, M., Sikorski, M.,  & Jaskolski, M. (2014). Inorganic pyrophosphatase (PPase)
from a higher plant. BioTechnologia, 94(1), 35-37. https://doi.org/10.5114/bta.2013.46433

Chicago

Grzechowiak, Marta, Michał Sikorski,  and Mariusz Jaskolski. 2014. "Inorganic pyrophosphatase (PPase)
from a higher plant". BioTechnologia 94 (1): 35-37. doi:10.5114/bta.2013.46433.

Harvard

Grzechowiak, M., Sikorski, M.,  and Jaskolski, M. (2014). Inorganic pyrophosphatase (PPase)
from a higher plant. BioTechnologia, 94(1), pp.35-37. https://doi.org/10.5114/bta.2013.46433

MLA

Grzechowiak, Marta et al. "Inorganic pyrophosphatase (PPase)
from a higher plant." BioTechnologia, vol. 94, no. 1, 2014, pp. 35-37. doi:10.5114/bta.2013.46433.

Vancouver

Grzechowiak M, Sikorski M, Jaskolski M. Inorganic pyrophosphatase (PPase)
from a higher plant. BioTechnologia. 2014;94(1):35-37. doi:10.5114/bta.2013.46433.

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.