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

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.

journal_name

J Mol Biol

authors

Jancarik J,Scott WG,Milligan DL,Koshland DE Jr,Kim SH

doi

10.1016/0022-2836(91)80198-4

keywords:

subject

Has Abstract

pub_date

1991-09-05 00:00:00

pages

31-4

issue

1

eissn

0022-2836

issn

1089-8638

pii

0022-2836(91)80198-4

journal_volume

221

pub_type

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