Purification, crystallization and preliminary X-ray analysis of aspartokinase III from Escherichia coli.

Blanco J; Viola RE

首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Purification, crystallization and preliminary X-ray analysis of aspartokinase III from Escherichia coli.

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Purification, crystallization and preliminary X-ray analysis of aspartokinase III from Escherichia coli.

机译：净化、结晶和初步的第三天冬氨酸激酶的x射线分析大肠杆菌。

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Aspartokinase III catalyzes the commitment step in the aspartate metabolism pathway, the phosphorylation of aspartic acid. The Escherichia coli enzyme has been crystallized in the presence of its natural substrate (aspartic acid) and Mg-ADP and diffraction data has been collected at a synchroton source. The crystals belong to the orthorhombic space group C222(1), with unit-cell parameters a = 60.44, b = 190.31, c = 99.55 A, and data 99.3% complete to 2.7 A. Solving the structure of AK III will provide the first structure of an aspartokinase from any organism.

机译：第三天冬氨酸激酶催化一步的承诺天冬氨酸代谢途径,天冬氨酸的磷酸化。杆菌酶已结晶的存在其天然底物(天冬氨酸)和Mg-ADP和衍射数据收集synchroton源。斜方晶系的空间群C222(1),与单胞参数= 60.44,= 190.31 b, c = 99.55,2.7数据99.3%完成。正义与发展党三世将提供第一个结构天冬氨酸激酶的结构从任何有机体。

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《Acta crystallographica.Section D. Biological crystallography》 |2002年第2期|352-354|共3页
作者
Blanco J; Viola RE;
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作者单位

Department of Chemistry, University of Toledo, 2801 West Bancroft Street, Toledo, Ohio 43606, USA.;

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正文语种英语
中图分类化学;
关键词
Escherichia coli; X-ray analysis; Aspartate KinaseAspartic Acid;

机译：大肠杆菌、x射线分析、天冬氨酸KinaseAspartic酸;

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Purification, crystallization and preliminary X-ray analysis of aspartokinase III from Escherichia coli.

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