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鼠伤寒沙门氏菌趋化作用介导的天冬氨酸受体配体结合结构域的结晶及初步X射线衍射研究

Crystallization and preliminary X-ray diffraction study of the ligand-binding domain of the bacterial chemotaxis-mediating aspartate receptor of Salmonella typhimurium.

作者信息

Jancarik J, Scott W G, Milligan D L, Koshland D E, Kim S H

机构信息

Department of Chemistry, University of California, Berkeley 94720.

出版信息

J Mol Biol. 1991 Sep 5;221(1):31-4. doi: 10.1016/0022-2836(91)80198-4.

DOI:10.1016/0022-2836(91)80198-4
PMID:1656050
Abstract

The periplasmic domain of the aspartate chemotaxis receptor from Salmonella typhimurium has been crystallized in the presence and absence of bound aspartate. Both crystal forms were grown by precipitation with lithium sulfate and diffract to 1.8 A resolution. The aspartate receptor structure is believed to be prototypical of a large class of receptors including those for polypeptide growth factor hormones as well as those for small chemotaxis-affector molecules such as aspartate and serine.

摘要

鼠伤寒沙门氏菌天冬氨酸趋化受体的周质结构域在结合和未结合天冬氨酸的情况下均已结晶。两种晶体形式均通过硫酸锂沉淀生长,衍射分辨率达到1.8埃。天冬氨酸受体结构被认为是一大类受体的原型,包括那些多肽生长因子激素受体以及那些小分子趋化影响分子(如天冬氨酸和丝氨酸)的受体。

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