Thin layers of water on biomolecular and other nanostructured surfaces can be supercooled to temperatures not accessible with bulk water. Chen et al. [PNAS 103, 9012 (2006)] suggested that anomalies near 220 K observed by quasi-elastic neutron scattering can be explained by a hidden critical point of bulk water. Based on more sensitive measurements of water on perdeuterated phycocyanin, using the new neutron backscattering spectrometer SPHERES, and an improved data analysis, we present results that show no sign of such a fragile-to-strong transition. The inflection of the elastic intensity at 220 K has a dynamic origin that is compatible with a calorimetric glass transition at 170 K. The temperature dependence of the relaxation times is highly sensitive to data evaluation; it can be brought into perfect agreement with the results of other techniques, without any anomaly. In contrast to bulk water, protein hydration water can be supercooled down to a glass transition at T g ≃ 170 K. Near T g translational degrees of freedom arrest, which induces discontinuities in the specific heat and the thermal expansion coefficient of the hydration water [1][2][3][4]. Due to the dynamic nature of the glass transition, freezing of microscopic degrees of freedom can already be observed far above T g .The protein dynamic transition is an abrupt onset of atomic displacements on the microscopic length and time scale probed by quasielastic neutron scattering (QENS). First observed twenty years ago in hydrated myoglobin and lysozyme at T ∆ ≃ 240 K [5], it is now known to be a generic property of hydrated proteins, while it is absent in dehydrated systems. It is therefore related to the dynamics of the hydration shell.In QENS, mean squared dispacements δx 2 are deduced from the elastic scattering intensity S(q, 0). Due to the finite spectrometer resolution (fwhm 2∆ω), one actually measures S(q, |ω| ∆ω). Full spectral measurements show that the anomalous decrease of the central peak is compensated by increasing inelastic wings [5,6]. These effects have been interpreted as precursors of the glass transition. Since QENS probes structural relaxation at ∆ω −1 ≃ 100 ps, while the calorimetric T g refers to a time scale of 100 s, it is natural that T ∆ is located far above T g : the protein dynamic transition is the microscopic manifestation of the glass transition in the hydration shell. The time-scale dependence of T ∆ also explains its variation with viscosity [7][8][9]. * Electronic address: wdoster@ph.tum.de Recently, these views have been challenged by the suggestion that there might be a time-scale independent transition. Support came mainly from QENS experiments on the backscattering spectrometer HFBS at NIST. In hydrated lysozyme, DNA and RNA, a kink was found not only in S(q, |ω| ∆ω), but also in the α relaxation time τ deduced from full spectra S(q, ω) [10][11][12][13]. This change of τ (T ) from high-T super-Arrhenius to low-T Arrhenius behavior at T L ≃ 220 K has been interpreted as a fragile-to-strong-transition (FST) from the...