Literature DB >> 3069841

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

Y Katsube1, N Tanaka, A Takenaka, T Yamada, T Oshima.   

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.

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Year:  1988        PMID： 3069841     DOI： 10.1093/oxfordjournals.jbchem.a122531

Source DB:  PubMed          Journal:  J Biochem        ISSN： 0021-924X            Impact factor:   3.387


  3 in total

1.  Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase.

Authors:  J H Hurley; P E Thorsness; V Ramalingam; N H Helmers; D E Koshland; R M Stroud
Journal:  Proc Natl Acad Sci U S A       Date:  1989-11       Impact factor: 11.205

2.  Crystallization and preliminary X-ray diffraction analysis of various enzyme-substrate complexes of isopropylmalate dehydrogenase from Thermus thermophilus.

Authors:  Angelo Merli; Karuppasamy Manikandan; Eva Gráczer; Linda Schuldt; Rajesh Kumar Singh; Péter Závodszky; Mária Vas; Manfred S Weiss
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2010-05-29

3.  Molecular cloning of the isocitrate dehydrogenase gene of an extreme thermophile, Thermus thermophilus HB8.

Authors:  K Miyazaki; H Eguchi; A Yamagishi; T Wakagi; T Oshima
Journal:  Appl Environ Microbiol       Date:  1992-01       Impact factor: 4.792
  3 in total

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