Homology models were built for
the 17 SCR domains and energy minimisations were
performed to improve the connectivity in the fh model.
triantennary complex-type carbohydrate structures
(MAN3GLCNAC6GAL3FUC3NEUNAC1) were added to each of the
N-linked glycosylation sites. a library of linker peptide
conformations was used in domain modelling constrained
by the solution scattering fits. modelling with the
scattering data was also carried out by rotational
search methods. the x-ray and neutron scattering curve
I(Q) was calculated assuming a uniform scattering density
for the spheres using the debye equation as adapted to
spheres. x-ray curves were calculated from the hydrated
sphere models without corrections for wavelength spread or
beam divergence, while these corrections were applied for
the neutron curves but now using unhydrated models.