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Bovine serum albumin (BSA) was dissolved in a mixture of deuterated glycerol and heavy water. The clusters formed by the 3300 proton spins in each BSA molecule were dynamically polarized up to P = 40%. Spin-contrast variation in small-angle neutron scattering was studied at several target polarizations. Zero contrast, and hence minimum polarized neutron small-angle scattering, is expected at PH = 60% from extrapolation of present data. The three basic scattering functions of spin-contrast variation look very similar because the shape of the BSA molecule and its proton distribution are congruent. Neutron smallangle scattering of BSA is similar to X-ray small-angle scattering at room temperature, indicating no deterioration of the molecular structure of BSA on solidification.

Polarised targets as used in high energy physics experiments may be of considerable interest in biological structure research using polarized neutrons. So far, this promising method has been facing difficulties in getting reasonable polarization of the target nuclei. We report on a polarized "frozen spin" target which has been prepared from an enzyme dissolved in a mixture of heavy water and deuterated propanediol doped with a completely deuterated paramagnetic radical. Clusters of 700 protons defined by the structure of lysozyme embedded in a fully deuterated matrix were polarized to 75% within an hour by 4 mm microwave irradiation in a magnetic field of 2.5 tesla at a temperature of 0.3 K. The polarisation behaviour of biological targets can be compared to the best frozen spin target materials in high energy physics research.