The sensitivity of Neutron Macromolecular Crystallography to the presence of hydrogen makes it a powerful tool to study protein structure. This technique is currently limited by the relative low neutron flux provided by even the most modern neutron sources. The strong polarization dependence of the neutron scattering cross section of hydrogen will allow Dynamic Nuclear Polarization to dramatically improve the sensitivity of protein structure measurements. This will enable the use of substantially smaller protein crystals, allowing structure measurements which are currently impossible. We present a proof of concept frozen spin target, built at Oak Ridge National Laboratory to polarize single protein crystals on the IMAGINE beamline at the High Flux Isotope Reactor. The results of the first test on the neutron beam will be discussed, as will planned upgrades to the system.