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Purification, crystallization and room-temperature X-ray diffraction of inositol dehydrogenase LcIDH2 from Lactobacillus casei BL23.
- Source :
-
Acta crystallographica. Section F, Structural biology communications [Acta Crystallogr F Struct Biol Commun] 2014 Jul; Vol. 70 (Pt 7), pp. 979-83. Date of Electronic Publication: 2014 Jun 19. - Publication Year :
- 2014
-
Abstract
- Lactobacillus casei BL23 contains two genes, iolG1 and iolG2, homologous with inositol dehydrogenase encoding genes from many bacteria. Inositol dehydrogenase catalyzes the oxidation of inositol with concomitant reduction of NAD+. The protein encoded by iolG2, LcIDH2, has been purified to homogeneity, crystallized and cryoprotected for diffraction at 77 K. The crystals had a high mosaicity and poor processing statistics. Subsequent diffraction measurements were performed without cryoprotectant at room temperature. These crystals were radiation-resistant and a full diffraction data set was collected at room temperature to 1.6 Å resolution.
- Subjects :
- Amino Acid Sequence
Bacterial Proteins genetics
Bacterial Proteins metabolism
Cloning, Molecular
Crystallization
Crystallography, X-Ray
Escherichia coli genetics
Escherichia coli metabolism
Gene Expression
Lacticaseibacillus casei enzymology
Molecular Sequence Data
Recombinant Proteins chemistry
Recombinant Proteins genetics
Recombinant Proteins metabolism
Sequence Alignment
Sequence Homology, Amino Acid
Sugar Alcohol Dehydrogenases genetics
Sugar Alcohol Dehydrogenases metabolism
Bacterial Proteins chemistry
Lacticaseibacillus casei chemistry
Sugar Alcohol Dehydrogenases chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 2053-230X
- Volume :
- 70
- Issue :
- Pt 7
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section F, Structural biology communications
- Publication Type :
- Academic Journal
- Accession number :
- 25005103
- Full Text :
- https://doi.org/10.1107/S2053230X14011595