Crystallization of bothropstoxin II isolated from the venom of Bothrops jararacussu.
A myotoxic phospholipase A2, bothropstoxin II, which exhibits low hydrolytic activity, was crystallized and X-ray diffraction data were collected to a resolution of 2.2 A. Preliminary analysis reveals the presence of three molecules in the asymmetric unit.
Bortoleto
R K
RK
Departamento de Fisica, Universidade Estadual Paulista, São Jose do Rio Preto, SP, Brazil.
Ward
R J
RJ
Giglio
J R
JR
Cintra
A C
AC
Arni
R K
RK
D000818:Animals; D017837:Bothrops; D003435:Crotalid Venoms / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D003460:Crystallization; D054501:Group II Phospholipases A2; D008970:Molecular Weight; D010741:Phospholipases A / Q000737:chemistry* / Q000302:isolation & purification; D054467:Phospholipases A2; D030162:Reptilian Proteins; D014961:X-Ray Diffraction
D003435:Crotalid Venoms; D030162:Reptilian Proteins; D010741:Phospholipases A; D054501:Group II Phospholipases A2; D054467:Phospholipases A2; C072031:bothropstoxin II