Two crystalline forms of GADPH (d-glyceraldehyde-3-phosphate dehydrogenase) from Spinacia oleracea were obtained using sitting-drop vapor diffusion. Despite the very low concentration of GADPH in the solutions, two crystalline forms were obtained, one of which was the previously reported C222 space group with unit-cell parameters a = 155.3, b = 181.7, c = 107.6 Å and the other of which belonged to a new space group I4122, with unit-cell parameters a = b = 120.9, c = 154.5 Å. Diffraction data were measured from both native and derivatives, yielding structures at a resolution limit of 3.0 Å. Differences at the NAD+/NADP+-binding site seen in these structures compared with the previously reported structure with bound coenzyme suggest that conformational changes associated with pyridine-nucleotide binding may play a role in the regulation of this enzyme.
|Number of pages||6|
|Journal||Acta Crystallographica Section F: Structural Biology and Crystallization Communications|
|Publication status||Published - Nov 2006|
- Glutamate synthase
ASJC Scopus subject areas
- Structural Biology
- Condensed Matter Physics