Preliminary X‐ray crystallographic analysis of tryptophanase from Escherichia coli

FEBS Letters

Tani, Shunsuke²  Sato, Mamoru¹  Kawata, Yasushi²  Tokushige, Masanobu²  Katsube, Yukiteru¹ 

[1] Institute for Protein Research, Osaka University, Suita, Osaka 565, Japan;Department of Chemistry, Faculty of Science, Kyoto University, Sakyo-ku, Kyoto 606, Japan

关键词: Tryptophanase;    L-Tryptophan indole-lyase: Crystal data;    Crystallization;    Escherichia coli;    PLP;    pyridoxal 5′ phosphate;   

DOI  :  10.1016/0014-5793(91)80701-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Tryptophanase (L-tryptophan indole-lyase) from Escherichia coli has been crystallized from ammonium sulfate solution using a vapor diffusion method. The crystals are tetragonal and belong to space group P4₁2₁2 or its enantiomorph. The cell dimensions of the crystals are a = b = 113.4 Å, and c = 232.2 Å, with two subunits per asymmetric unit. The crystals diffract to at least 3 Å resolution, and are suitable for X-ray structural analysis.

【 授权许可】

Unknown