| Literature DB >> 23908034 |
Mayumi Niiyama1, Shigeru Sugiyama, Mika Hirose, Sae Ishikawa, Hideyuki Tomitori, Kyohei Higashi, Tomoko Yamashita, Hiroaki Adachi, Kazufumi Takano, Satoshi Murakami, Michio Murata, Tsuyoshi Inoue, Yusuke Mori, Keiko Kashiwagi, Hiroyoshi Matsumura, Kazuei Igarashi.
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.Entities:
Keywords: Escherichia coli; spermidine acetyltransferase
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Year: 2013 PMID： 23908034 PMCID： PMC3729165 DOI： 10.1107/S1744309113017132
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN： 1744-3091