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 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.
authors.affiliation: Bioscience Division, MS M888, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.
authors.forename: A Y
authors.initials: AY
authors.lastname: Kovalevsky
authors.forename: S Zoe
authors.initials: SZ
authors.lastname: Fisher
authors.forename: Sean
authors.initials: S
authors.lastname: Seaver
authors.forename: Marat
authors.initials: M
authors.lastname: Mustyakimov
authors.forename: Narayanasami
authors.initials: N
authors.lastname: Sukumar
authors.forename: Paul
authors.initials: P
authors.lastname: Langan
authors.forename: Timothy C
authors.initials: TC
authors.lastname: Mueser
authors.forename: B Leif
authors.initials: BL
authors.lastname: Hanson
mesh_terms: D000818:Animals; D018360:Crystallography, X-Ray; D006736:Horses; D008706:Methemoglobin / Q000031:analogs & derivatives* / Q000737:chemistry; D008958:Models, Molecular; D033363:Neutron Diffraction; D017434:Protein Structure, Tertiary
chemical_list: C007169:cyanomethemoglobin; D008706:Methemoglobin
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