Protein crystallography is an established technique for determining the structure of many protein systems. X-ray protein crystallography is the dominant technique, as the incredibly high flux of modern light sources allows researchers to collect data very quickly using very small crystals. In comparison, neutron crystallography has many unique advantages (due the neutron’s sensitivity to isotopes and light nuclei) but suffers from the low flux available at neutron sources. The spin dependence of slow neutron scattering provides an opportunity to overcome the flux limitations of neutron sources, expanding the number of protein systems that can be studied, improving the signal to noise, and enabling novel measurement techniques to determine the location of hydrogen atoms. At Oak Ridge National Laboratory, a program has been underway to develop Dynamic Nuclear Polarization (DNP) techniques, and apply them to neutron scattering, especially Neutron Macromolecular Crystallography of proteins. The status and results of the Dynamic Nuclear Polarization program at Oak Ridge National Laboratory will be discussed, with an emphasis on the use of DNP to enhance measurements of diffraction from protein crystals.