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...

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Detaylı Bibliyografya
Asıl Yazarlar: Shibata, Naoki, Tamagaki, Hiroko, Ohtsuki, Shungo, Hieda, Naoki, Akita, Keita, Komori, Hirofumi, Shomura, Yasuhito, Terawaki, Shin-ichi, Toraya, Tetsuo, Yasuoka, Noritake, Higuchi, Yoshiki
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: International Union of Crystallography 2010
Konular:
Crystallization Communications
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC2882776/
https://ncbi.nlm.nih.gov/pubmed/20516606
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309110014478
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