The structure of spinach light-harvesting complex II (LHC II), stabilized in a solution of the detergent n-octyl-beta-D-glucoside (BOG), was investigated by small-angle neutron scattering (SANS). Physicochemical characterization of the isolated complex indicated that it was pure (>95%) and also in its native trimeric state. SANS with contrast variation was used to investigate the properties of the protein-detergent complex at three different H2O/D2O contrast match points, enabling the scattering properties of the protein and detergent to be investigated independently. The topological shape of LHC 11, determined using ab initio shape restoration methods from the SANS data at the contrast match point of BOG, was consistent with the X-ray crystallographic structure of LHC 11 (Liu et al. Nature 2004 428, 287-292). The interactions of the protein and detergent were investigated at the contrast match point for the protein and also in 100% D2O. The data suggested that BOG micelle structure was altered by its interaction with LHC 11, but large aggregate structures were not Formed. Indirect Fourier transform analysis of the LHC II/BOG scattering curves showed that the increase in the maximum dimension of the protein-detergent complex was consistent with the presence of a monolayer of detergent Surrounding the protein. A model of the LHC II/BOG complex was generated to interpret the measurements made in 100% D2O. This model adequately reproduced the overall size of the LHC II/BOG complex, but demonstrated that the detergent does not have a highly regular shape that surrounds the hydrophobic periphery of LHC II. In addition to demonstrating that natively Structured LHC 11 can be produced for functional characterization and for use in artificial solar energy applications, the analysis and modeling approaches described here can be used for characterizing detergent-associated alpha-helical transmembrane proteins.