The glycosylation of glycoproteins is a major determinant of their stability, and glycans also affect their aggregatibility (precipitation). An understanding of this is essential for improving manufacturing processes. Our extensive background in glycosylation and scattering (see below) indicates that we are ideally positioned to investigate antibody glycan structures in detail. We will compare both glycosylated and deglycosylated IgG antibodies using a combination of neutron and X-ray scattering, ultracentrifugation and modelling. The two overall aims of this project are to (i) identify how the solution properties of glycans affect antibody manufacture and (ii) develop a pipeline of new methods for the rapid atomistic modelling of antibody conformations based on neutron and X-ray scattering fits in order to evaluate the manufacturability of variously glycosylated antibodies.