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.