Archaeoglobus fulgidus, a hyperthermophilic archaeon, accumulates di-myo-inositol phosphate (DIP) in response to heat stress. Recently, the pathway for biosynthesis of DIP has been elucidated in this organism and involves a bifunctional enzyme that contains two domains: CTP:inositol-1- phosphate cytidylyltransferase (IPCT) as a soluble domain and di-myo-inositol-1,3′-phosphate-1-phosphate synthase (DIPPS) as a membrane domain. Here, the expression, purification, crystallization and preliminary X-ray diffraction analysis of the IPCT domain from A. fulgidus in the apo form are reported. The crystals diffracted to 2.4 Å resolution using a synchrotron source and belonged to the orthorhombic space group P21212, with unit-cell parameters a = 154.7, b = 83.9, c = 127.7 Å. © 2010 International Union of Crystallography All rights reserved.
CITATION STYLE
Brito, J. A., Borges, N., Santos, H., & Archer, M. (2010). Production, crystallization and preliminary X-ray analysis of CTP:inositol-1-phosphate cytidylyltransferase from Archaeoglobus fulgidus. In Acta Crystallographica Section F: Structural Biology and Crystallization Communications (Vol. 66, pp. 1463–1465). https://doi.org/10.1107/S1744309110032677
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