The locations of H atoms in biological structures can be difficult to determine using X-ray diffraction methods. Neutron diffraction offers a relatively greater scattering magnitude from H and D atoms. Here, 1.65β
Γ
resolution neutron diffraction studies of fully perdeuterated and selectively CH~3~-protonated perdeuterated crystals of__Pyrococcus furiosus__rubredoxin (D-rubredoxin and HD-rubredoxin, respectively) at room temperature (RT) are described, as well as 1.1β
Γ
resolution X-ray diffraction studies of the same protein at both RT and 100β
K. The two techniques are quantitatively compared in terms of their power to directly provide atomic positions for D atoms and analyze the role played by atomic thermal motion by computing the Ο level at the D-atom coordinate in simulated-annealing composite D-OMIT maps. It is shown that 1.65β
Γ
resolution RT neutron data for perdeuterated rubredoxin are βΌ8 times more likely overall to provide high-confidence positions for D atoms than 1.1β
Γ
resolution X-ray data at 100β
K or RT. At or above the 1.0Ο level, the joint X-ray/neutron (XN) structures define 342/378 (90%) and 291/365 (80%) of the D-atom positions for D-rubredoxin and HD-rubredoxin, respectively. The X-ray-only 1.1β
Γ
resolution 100β
K structures determine only 19/388 (5%) and 8/388 (2%) of the D-atom positions above the 1.0Ο level for D-rubredoxin and HD-rubredoxin, respectively. Furthermore, the improved model obtained from joint XN refinement yielded improved electron-density maps, permitting the location of more D atoms than electron-density maps from models refined against X-ray data only.