Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 64, Part 2 (February 2008)

crystallization communications


HTML versionpdf version buy article online

Acta Cryst. (2008). F64, 98-101    [ doi:10.1107/S1744309108000328 ]

Purification, crystallization and preliminary X-ray analysis of inositol dehydrogenase (IDH) from Bacillus subtilis

K. E. Van Straaten, A. Hoffort, D. R. J. Palmer and D. A. R. Sanders

Abstract: 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 Ni2+-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 I222 and contain one molecule per asymmetric unit.

Keywords: inositol dehydrogenases; Bacillus subtilis.

 bibliographic record in  format
  Find reference:   Volume   Page   
  Search:     From   to      Advanced search

Copyright © International Union of Crystallography
IUCr Webmaster