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Expression, purification, crystallization and preliminary crystallographic analysis of spermidine acetyltransferase from Escherichia coli.


ABSTRACT: The spermidine acetyltransferase (SAT) from Escherichia coli catalyses the transfer of acetyl groups from acetyl-CoA to spermidine. SAT has been expressed and purified from E. coli. SAT was crystallized by the sitting-drop vapour-diffusion method to obtain a more detailed insight into the molecular mechanism. Preliminary X-ray diffraction studies revealed that the crystals diffracted to 2.5 Å resolution and belonged to the cubic space group P23, with unit-cell parameters a = b = c = 148.7 Å. They contained four molecules per asymmetric unit.

SUBMITTER: Niiyama M 

PROVIDER: S-EPMC3729165 | biostudies-other | 2013 Aug

REPOSITORIES: biostudies-other

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Expression, purification, crystallization and preliminary crystallographic analysis of spermidine acetyltransferase from Escherichia coli.

Niiyama Mayumi M   Sugiyama Shigeru S   Hirose Mika M   Ishikawa Sae S   Tomitori Hideyuki H   Higashi Kyohei K   Yamashita Tomoko T   Adachi Hiroaki H   Takano Kazufumi K   Murakami Satoshi S   Murata Michio M   Inoue Tsuyoshi T   Mori Yusuke Y   Kashiwagi Keiko K   Matsumura Hiroyoshi H   Igarashi Kazuei K  

Acta crystallographica. Section F, Structural biology and crystallization communications 20130727 Pt 8


The spermidine acetyltransferase (SAT) from Escherichia coli catalyses the transfer of acetyl groups from acetyl-CoA to spermidine. SAT has been expressed and purified from E. coli. SAT was crystallized by the sitting-drop vapour-diffusion method to obtain a more detailed insight into the molecular mechanism. Preliminary X-ray diffraction studies revealed that the crystals diffracted to 2.5 Å resolution and belonged to the cubic space group P23, with unit-cell parameters a = b = c = 148.7 Å. The  ...[more]

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