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

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

doi:10.1093/oxfordjournals.jbchem.a122531

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

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

Authors

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

Affiliation

¹ Institute of Protein Research, Osaka University.

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

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

3-Isopropylmalate Dehydrogenase
Alcohol Oxidoreductases / analysis*
Crystallization
Escherichia coli / genetics
Recombinant Proteins
Thermus / enzymology
X-Ray Diffraction

Substances

Recombinant Proteins
Alcohol Oxidoreductases
3-Isopropylmalate Dehydrogenase