@Article{Grzechowiak2013,
journal="BioTechnologia",
issn="0860-7796",
volume="94",
number="1",
year="2013",
title="Inorganic pyrophosphatase (PPase)
from a higher plant",
abstract=" 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 Ni 2+ -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.",
author="Grzechowiak, Marta
and Sikorski, Michał
and Jaskolski, Mariusz",
pages="35--37",
doi="10.5114/bta.2013.46433",
url="http://dx.doi.org/10.5114/bta.2013.46433"
}