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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 4(66), p. 474-477, 2010

DOI: 10.1107/s1744309110007840

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Preliminary neutron and X-ray crystallographic studies of equine cyanomethemoglobin

Journal article published in 2010 by A. Y. Kovalevsky, S. Zoe Fisher, S. Zoe Fisher, Sean Seaver, Marat Mustyakimov, Narayanasami Sukumar, Paul Langan ORCID, Timothy C. Mueser, B. Leif Hanson, B. Leif Hanson
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This paper is available in a repository.

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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.