Open AccessPreliminary neutron and X‐ray crystallographic studies of equine cyanomethemoglobin
Author(s) -
Kovalevsky A. Y.,
Fisher S. Zoe,
Seaver Sean,
Mustyakimov Marat,
Sukumar Narayanasami,
Langan Paul,
Mueser Timothy C.,
Hanson B. Leif
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110007840
Subject(s) - crystallography , x ray , materials science , neutron , chemistry , physics , nuclear physics
Room‐temperature and 100 K X‐ray and room‐temperature neutron diffraction data have been measured from equine cyanomethemoglobin to 1.7 Å resolution using a home source, to 1.6 Å resolution on NE‐CAT at the Advanced Photon Source and to 2.0 Å 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.