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                <term xml:lang="en">ultralow-temperature X-ray crystallography</term>
                <term xml:lang="en">crystal microspectroscopy</term>
                <term xml:lang="en">Neuroprotection</term>
                <term xml:lang="en">CO photolysis</term>
                <term xml:lang="en">Structure determination</term>
                <term xml:lang="en">Protein structure</term>
                <term xml:lang="en">oxygen binding</term>
                <term xml:lang="en">soak-and-freeze pressurization</term>
                <term xml:lang="en">structural biology</term>
                <term xml:lang="en">cryo-trapping</term>
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              <p>A combined biophysical approach was applied to map gas-docking sites within murine neuroglobin (Ngb), revealing snapshots of events that might govern activity and dynamics in this unique hexacoordinate globin, which is most likely to be involved in gas-sensing in the central nervous system and for which a precise mechanism of action remains to be elucidated. The application of UV-visible microspectroscopy in crystallo, solution X-ray absorption near-edge spectroscopy and X-ray diffraction experiments at 15-40 K provided the structural characterization of an Ngb photolytic intermediate by cryo-trapping and allowed direct observation of the relocation of carbon monoxide within the distal heme pocket after photodissociation. Moreover, X-ray diffraction at 100 K under a high pressure of dioxygen, a physiological ligand of Ngb, unravelled the existence of a storage site for O2 in Ngb which coincides with Xe-III, a previously described docking site for xenon or krypton. Notably, no other secondary sites were observed under our experimental conditions.</p>
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