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Purification, crystallization and room‐temperature X‐ray diffraction of inositol dehydrogenase LcIDH2 from Lactobacillus casei BL23
Author(s) -
Bertwistle Drew,
Vogt Linda,
Aamudalapalli Hari Babu,
Palmer David R. J.,
Sanders David A. R.
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14011595
Subject(s) - dehydrogenase , lactobacillus casei , nad+ kinase , inositol , crystallization , x ray crystallography , alcohol dehydrogenase , diffraction , biology , chemistry , biochemistry , crystallography , enzyme , fermentation , optics , physics , receptor , organic chemistry
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.