Crystallization and preliminary X-ray diffraction analysis of myotoxin I, a Lys49-phospholipase A2 from Bothrops moojeni

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
D P Marchi-SalvadorM R M Fontes

Abstract

A new myotoxic Lys49-phospholipase A2 isolated from Bothrops moojeni snake venom has been crystallized. The crystals diffracted to 2.18 A resolution using a synchrotron-radiation source and belong to space group C2. The unit-cell parameters are a = 56.8, b = 125.0, c = 64.7 A, beta = 105.5 degrees. Preliminary analysis indicates the presence of four molecules in the asymmetric unit. This may suggest a new quaternary structure for this Lys49-phospholipase A2 in contrast to the dimeric and monomeric structures solved so far for this class of proteins.

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Citations

Jun 7, 2006·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·D P Marchi-SalvadorM R M Fontes
Aug 2, 2006·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·L C CorrêaM R M Fontes
Jan 31, 2006·Comparative Biochemistry and Physiology. Toxicology & Pharmacology : CBP·Rodrigo G StábeliAndreimar M Soares
Dec 29, 2009·Toxicon : Official Journal of the International Society on Toxinology·Anna Maria PerchucReto Stöcklin
May 13, 2008·Toxicon : Official Journal of the International Society on Toxinology·Laure MeninReto Stöcklin

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