| Literature DB >> 20383026 |
A Y Kovalevsky1, S Zoe Fisher, Sean Seaver, Marat Mustyakimov, Narayanasami Sukumar, Paul Langan, Timothy C Mueser, B Leif Hanson.
Abstract
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.Entities:
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Year: 2010 PMID: 20383026 PMCID: PMC2852348 DOI: 10.1107/S1744309110007840
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091