Expression, crystallization and preliminary X-ray crystallographic study of ethanolamine ammonia-lyase from Escherichia coli

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 66; no. 6; pp. 709 - 711
• Main Authors: Shibata, Naoki, Tamagaki, Hiroko, Ohtsuki, Shungo, Hieda, Naoki, Akita, Keita, Komori, Hirofumi, Shomura, Yasuhito, Terawaki, Shin-ichi, Toraya, Tetsuo, Yasuoka, Noritake, Higuchi, Yoshiki
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.06.2010
• Subjects: adenosylcobalamin; Crystallization; Crystallization Communications; Crystallography, X-Ray; Escherichia coli; Escherichia coli - enzymology; ethanolamine ammonia-lyase; Ethanolamine Ammonia-Lyase - chemistry; Ethanolamine Ammonia-Lyase - genetics; Gene Expression; Mutation; radical enzymes
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S1744309110014478

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.