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. 2007 Jul 1;63(Pt 7):553-5.
doi: 10.1107/S1744309107023512. Epub 2007 Jun 11.

Crystallization and preliminary X-ray diffraction analysis of the hyperthermophilic Sulfolobus solfataricus phosphotriesterase

Mikael Elias  1 , Jérôme Dupuy, Luigia Merone, Claude Lecomte, Mosè Rossi, Patrick Masson, Giuseppe Manco, Eric Chabriere
Affiliations

Crystallization and preliminary X-ray diffraction analysis of the hyperthermophilic Sulfolobus solfataricus phosphotriesterase

Mikael Elias et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

Abstract

Organophosphates constitute the largest class of insecticides used worldwide and some of them are potent nerve agents. Consequently, organophosphate-degrading enzymes are of paramount interest as they could be used as bioscavengers and biodecontaminants. Phosphotriesterases (PTEs) are capable of hydrolyzing these toxic compounds with high efficiency. A distant and hyperthermophilic representative of the PTE family was cloned from the archeon Sulfolobus solfataricus MT4, overexpressed in Escherichia coli and crystallized; the crystals diffracted to 2.54 A resolution. Owing to its exceptional thermostability, this PTE may be an excellent candidate for obtaining an efficient organophosphate biodecontaminant. Here, the crystallization conditions and data collection for the hyperthermophilic S. solfataricus PTE are reported.

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Figures

Figure 1
Figure 1
Typical crystal of the hyperthermophilic phosphotriesterase from S. solfataricus.
Figure 2
Figure 2
A diffraction pattern of a crystal of the phosphotriesterase from S. solfataricus. The edge of the frame is at 2.1 Å.
See this image and copyright information in PMC

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