The sensitivity of Neutron Macromolecular Crystallography to the presence of hydrogen makes it a powerful tool to
compliment X-ray crystallographic studies using protein crystals. The power of this technique is currently limited by
the relative low neutron flux provided by even the most powerful neutron sources. The strong polarization dependence
of the neutron scattering cross section of hydrogen will allow us to use Dynamic Nuclear Polarization to dramatically
improve the sensitivity of these measurements, and enable measurements of protein structures that are currently impossible.
We present a prototype frozen spin system, built at Oak Ridge National Laboratory to polarize single protein
crystals on the IMAGINE beamline at the High Flux Isotope Reactor (HFIR). Details of the design and construction
will be described, as will the performance of the system oine and during tests at HFIR.