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

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.

SUBMITTER: Marchi-Salvador DP

PROVIDER: S-EPMC1991306 | biostudies-literature | 2005 Oct

REPOSITORIES: biostudies-literature

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

Marchi-Salvador D P DP Silveira L B LB Soares A M AM Fontes M R M MR

Acta crystallographica. Section F, Structural biology and crystallization communications 20050913 Pt 10

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 monomer ...[more]

PMID: 16511185

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