Preliminary neutron and X-ray crystallographic studies of equine cyanomethemoglobin.
Publication Type:Journal Article
Source:Acta Crystallogr Sect F Struct Biol Cryst Commun, Volume 66, Issue Pt 4, p.474-7 (2010)
Keywords:Animals, Crystallography, X-Ray, Horses, Methemoglobin, Models, Molecular, Neutron Diffraction, Protein Structure, Tertiary
<p>Room-temperature and 100 K X-ray and room-temperature neutron diffraction data have been measured from equine cyanomethemoglobin to 1.7 A resolution using a home source, to 1.6 A resolution on NE-CAT at the Advanced Photon Source and to 2.0 A resolution on the PCS at Los Alamos Neutron Science Center, respectively. The cyanomethemoglobin is in the R state and preliminary room-temperature electron and neutron scattering density maps clearly show the protonation states of potential Bohr groups. Interestingly, a water molecule that is in the vicinity of the heme group and coordinated to the distal histidine appears to be expelled from this site in the low-temperature structure.</p>