Open AccessExpression, purification, crystallization and preliminary crystallographic analysis of spermidine acetyltransferase from Escherichia coli
Author(s) -
Niiyama Mayumi,
Sugiyama Shigeru,
Hirose Mika,
Ishikawa Sae,
Tomitori Hideyuki,
Higashi Kyohei,
Yamashita Tomoko,
Adachi Hiroaki,
Takano Kazufumi,
Murakami Satoshi,
Murata Michio,
Inoue Tsuyoshi,
Mori Yusuke,
Kashiwagi Keiko,
Matsumura Hiroyoshi,
Igarashi Kazuei
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113017132
Subject(s) - spermidine , escherichia coli , crystallization , acetyltransferase , resolution (logic) , crystallography , chemistry , molecule , biochemistry , enzyme , organic chemistry , gene , acetylation , artificial intelligence , computer science
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 P 23, with unit‐cell parameters a = b = c = 148.7 Å. They contained four molecules per asymmetric unit.