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