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Crystallization and preliminary X-ray data for 3-isopropylmalate dehydrogenase of Thermus thermophilus.

作者信息

Katsube Y, Tanaka N, Takenaka A, Yamada T, Oshima T

机构信息

Institute of Protein Research, Osaka University.

出版信息

J Biochem. 1988 Nov;104(5):679-80. doi: 10.1093/oxfordjournals.jbchem.a122531.

DOI:10.1093/oxfordjournals.jbchem.a122531
PMID:3069841
Abstract

The gene coding for 3-isopropylmalate dehydrogenase of Thermus thermophilus was cloned and expressed in Escherichia coli. The extracted enzyme was crystallized in a suitable size for X-ray crystallographic studies. The crystals have a space group of P3(1)21 or P3(2)21 with a = b = 78.6 A and c = 157.4 A.

摘要

相似文献

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引用本文的文献

1
Crystallization and preliminary X-ray diffraction analysis of various enzyme-substrate complexes of isopropylmalate dehydrogenase from Thermus thermophilus.嗜热栖热菌异丙基苹果酸脱氢酶各种酶-底物复合物的结晶及初步X射线衍射分析
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2
Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase.由磷酸化作用调控的细菌酶——异柠檬酸脱氢酶的结构。
Proc Natl Acad Sci U S A. 1989 Nov;86(22):8635-9. doi: 10.1073/pnas.86.22.8635.
3
Molecular cloning of the isocitrate dehydrogenase gene of an extreme thermophile, Thermus thermophilus HB8.
嗜热栖热菌HB8异柠檬酸脱氢酶基因的分子克隆
Appl Environ Microbiol. 1992 Jan;58(1):93-8. doi: 10.1128/aem.58.1.93-98.1992.