Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 61, Part 10 (October 2005)

crystallization communications

Acta Cryst. (2005). F61, 882-884 [ doi:10.1107/S174430910502717X ]

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

D. P. Marchi-Salvador, L. B. Silveira, A. M. Soares and M. 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 Å 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 Å, [beta] = 105.5°. 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.

Keywords: myotoxin-I; Lys49-phospholipase A₂.