Preliminary X-ray crystallographic analysis of tryptophanase from Escherichia coli.
作者信息
Kawata Y, Tani S, Sato M, Katsube Y, Tokushige M
机构信息
Department of Chemistry, Faculty of Science, Kyoto University, Japan.
出版信息
FEBS Lett. 1991 Jun 24;284(2):270-2. doi: 10.1016/0014-5793(91)80701-4.
PMID:2060649
Abstract
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 P4(1)2(1)2 or its enantiomorph. The cell dimensions of the crystals are a = b = 113.4 A, and c = 232.2 A, with two subunits per asymmetric unit. The crystals diffract to at least 3 A resolution, and are suitable for X-ray structural analysis.
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