SAXS study of crotapotin at low pH.
The structure of crotapotin, a protein extracted, from the venom of the Crotalus durissus terrificus, in solution at pH = 1.5, was studied by SAXS. The experimental results yield structural parameter values of the molecular radius of gyration Rg = 13.6 A, volume v = 16.2 x 10(3) A3 A3 and maximal dimension Dmax = 46 A. The distance distribution function deduced from the scattering measurements is consistent with an overall molecular shape of an oblate ellipsoid of revolution with asymmetry parameter v = 0.45.
Abrego
J R
JR
Departamento de Física, Letras e Ciências Exatas/UNESP, SP, Brasil.
Craievich
A F
AF
Mascarenhas
Y P
YP
Laure
C J
CJ
D000818:Animals; D055592:Biophysical Phenomena; D001703:Biophysics; D003439:Crotoxin / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D012542:Scattering, Radiation; D012996:Solutions; D014965:X-Rays
D012996:Solutions; D003439:Crotoxin