Crystallization of piratoxin I, a myotoxic Lys49-phospholipase A2 homologue isolated from the venom of Bothrops pirajai.
Large single crystals of piratoxin I. a Lys49-PLA2 homologue with low enzymatic activity, have been obtained. The crystals belong to the orthorhombic system space group P2(1)2(1)2(1), and diffract X-rays to a resolution of 2.8 A. Preliminary analysis reveals the presence of two molecules in the crystallographic asymmetric unit.
Canduri
F
F
Departamento de Física, IBILCE/UNESP, São José do Rio Preto, SP, Brazil.
Mancuso
L C
LC
Soares
A M
AM
Giglio
J R
JR
Ward
R J
RJ
Arni
R K
RK
D000818:Animals; D017837:Bothrops; D003435:Crotalid Venoms / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D054501:Group II Phospholipases A2; D009498:Neurotoxins / Q000737:chemistry*; D010741:Phospholipases A / Q000032:analysis* / Q000737:chemistry* / Q000302:isolation & purification; D054467:Phospholipases A2; D030162:Reptilian Proteins
D003435:Crotalid Venoms; D009498:Neurotoxins; D030162:Reptilian Proteins; C114085:piratoxin I; D010741:Phospholipases A; D054501:Group II Phospholipases A2; D054467:Phospholipases A2; C061056:myotoxin II, Bothrops asper