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Purification, crystallization and room-temperature X-ray diffraction of inositol dehydrogenase LcIDH2 from Lactobacillus casei BL23.

Authors :
Bertwistle D
Vogt L
Aamudalapalli HB
Palmer DR
Sanders DA
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.

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