Open AccessPurification, crystallization and preliminary X‐ray analysis of inositol dehydrogenase (IDH) from Bacillus subtilis
Author(s) -
Van Straaten K. E.,
Hoffort A.,
Palmer D. R. J.,
Sanders D. A. R.
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108000328
Subject(s) - bacillus subtilis , dehydrogenase , inositol , nad+ kinase , crystallization , enzyme , resolution (logic) , chemistry , affinity chromatography , crystallography , biochemistry , biology , bacteria , organic chemistry , genetics , receptor , artificial intelligence , computer science
Inositol dehydrogenase (IDH) is an enzyme that catalyses the NAD + ‐dependent oxidation of myo ‐inositol to scyllo ‐inosose. The enzyme has been purified to homogeneity by means of Ni 2+ ‐affinity chromatography and was crystallized in both native and selenomethionine (SeMet) labelled forms using the microbatch method. SAD X‐ray diffraction data were collected to 2.0 Å resolution from a SeMet‐labelled crystal at the Advanced Photon Source (APS) and a MAD data set was collected to 1.75 Å resolution at the Canadian Light Source (CLS); this is the first reported anomalous diffraction experiment from the CLS. The crystals belong to space group I 222 and contain one molecule per asymmetric unit.