Open AccessExpression, crystallization and preliminary X‐ray crystallographic study of ethanolamine ammonia‐lyase from Escherichia coli
Author(s) -
Shibata Naoki,
Tamagaki Hiroko,
Ohtsuki Shungo,
Hieda Naoki,
Akita Keita,
Komori Hirofumi,
Shomura Yasuhito,
Terawaki Shinichi,
Toraya Tetsuo,
Yasuoka Noritake,
Higuchi Yoshiki
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110014478
Subject(s) - ethanolamine , escherichia coli , crystallization , enzyme , ammonia , lyase , solubility , chemistry , crystallography , biochemistry , organic chemistry , gene
Ethanolamine ammonia‐lyase (EAL) catalyzes the adenosylcobalamin‐dependent conversion of ethanolamine to acetaldehyde and ammonia. The wild‐type enzyme shows a very low solubility. N‐terminal truncation of the Escherichia coli EAL β‐subunit dramatically increases the solubility of the enzyme without altering its catalytic properties. Two deletion mutants of the enzyme [EAL(βΔ4–30) and EAL(βΔ4–43)] have been overexpressed, purified and crystallized using the sitting‐drop vapour‐diffusion method. Crystals of EAL(βΔ4–30) and EAL(βΔ4–43) diffracted to approximately 8.0 and 2.1 Å resolution, respectively.