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Crystallization and preliminary X-ray studies of a Bacillus subtilis and Thermus thermophilus HB8 chimeric 3-isopropylmalate dehydrogenase.
- Source :
-
Journal of biochemistry [J Biochem] 1991 Jan; Vol. 109 (1), pp. 1-2. - Publication Year :
- 1991
-
Abstract
- A chimeric gene was constructed by fusing the Bacillus subtilis and Thermus thermophilus genes coding for 3-isopropylmalate dehydrogenase, and expressed in Escherichia coli. The chimeric enzyme was crystallized in a size suitable for X-ray structure analysis. The crystal has a space group of P3(1)21 or P3(2)21, a = b = 77.1 A and c = 158.3 A, which is isomorphous with that of the native enzyme from T. thermophilus.
- Subjects :
- 3-Isopropylmalate Dehydrogenase
Alcohol Oxidoreductases chemistry
Bacillus subtilis enzymology
Bacillus subtilis genetics
Cloning, Molecular
Crystallization
Recombinant Proteins chemistry
Recombinant Proteins genetics
Thermus enzymology
Thermus genetics
X-Ray Diffraction
Alcohol Oxidoreductases genetics
Subjects
Details
- Language :
- English
- ISSN :
- 0021-924X
- Volume :
- 109
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Journal of biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 1901851
- Full Text :
- https://doi.org/10.1093/oxfordjournals.jbchem.a123328