Water plays a critical role in life. A hydration level, h ~ 0.2 g water/g protein, is found to be the minimum for the dynamical transition in protein at Td ~ 200 K. This temperature is universal for proteins and ascribed to the surface hydration water. However, our OSIRIS neutron data on perdeuterated cytochrome P450 (CYP) and its hydrogenated counterpart showed that the Td of hydration water shifts significantly to higher values when decreasing the instrument resolution, while the Td for the protein remains essentially unchanged. OSIRIS afforded us two resolutions (25.4 and 99 ueV) which we added to data from HFBS at NIST at 1ueV resolution. These results suggests that the dynamical transition might have a different physical origin from that of its surface water. To further confirm these findings, we want to try a structurally and functionally different protein, GFP, at OSIRIS.