Open AccessCrystallization and preliminary X‐ray analysis of CTP:phosphoethanolamine cytidylyltransferase (ECT) from Saccharomyces cerevisiae
Author(s) -
Lee Woo Cheol,
Nagata Koji,
Ohtsuka Jun,
Ono Yusuke,
Fukuda Ryouichi,
Ohta Akinori,
Tanokura Masaru
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106035561
Subject(s) - saccharomyces cerevisiae , crystallization , tetragonal crystal system , solvent , chemistry , peg ratio , phosphatidylethanolamine , enzyme , crystallography , x ray crystallography , biochemistry , diffraction , organic chemistry , crystal structure , yeast , phospholipid , physics , finance , membrane , phosphatidylcholine , optics , economics
CTP:phosphoethanolamine cytidylyltransferase (ECT) is the enzyme that catalyzes the conversion of phosphoethanolamine to CDP‐ethanolamine in the phosphatidylethanolamine‐biosynthetic pathway (Kennedy pathway). ECT from Saccharomyces cerevisiae was crystallized by the sitting‐drop vapour‐diffusion method using PEG 4000 as precipitant. The crystals diffracted X‐rays from a synchrotron‐radiation source to 1.88 Å resolution. The space group was assigned as primitive tetragonal, P 4 1 2 1 2 or P 4 3 2 1 2, with unit‐cell parameters a = b = 66.3, c = 150.8 Å. The crystals contain one ECT molecule in the asymmetric unit ( V M = 2.2 Å 3 Da −1 ), with a solvent content of 43%.