@article{98554869c40740788eedbe41accf3c9c,
title = "Preliminary neutron and X-ray crystallographic studies of equine cyanomethemoglobin",
abstract = "Room-temperature and 100 K X-ray and room-temperature neutron diffraction data have been measured from equine cyanomethemoglobin to 1.7 {\AA} resolution using a home source, to 1.6 {\AA} resolution on NE-CAT at the Advanced Photon Source and to 2.0 {\AA} 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.",
keywords = "Equine hemoglobin, Joint XN refinement, Protonation, R state, Time-of-flight neutron diffraction",
author = "Kovalevsky, {A. Y.} and Fisher, {S. Zoe} and Sean Seaver and Marat Mustyakimov and Narayanasami Sukumar and Paul Langan and Mueser, {Timothy C.} and Hanson, {B. Leif}",
year = "2010",
doi = "10.1107/S1744309110007840",
language = "English",
volume = "66",
pages = "474--477",
journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",
issn = "1744-3091",
number = "4",
}