Preliminary neutron and X-ray crystallographic studies of equine cyanomethemoglobin

Journal Article · Wed Aug 18 00:00:00 EDT 2010 · Acta Crystallogr. F

DOI:https://doi.org/10.1107/S1744309110007840· OSTI ID:1002354

Kovalevsky, A Y; Fisher, S Z; Seaver, S; Mustyakimov, M; Sukumar, N; Langan, P; Mueser, T C; Hanson, B L ^[1]

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1. Toledo

Room-temperature and 100 K X-ray and room-temperature neutron diffraction data have been measured from equine cyanomethemoglobin to 1.7 {angstrom} resolution using a home source, to 1.6 {angstrom} resolution on NE-CAT at the Advanced Photon Source and to 2.0 {angstrom} 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.

• Research Organization: Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
• Sponsoring Organization: USDOE
• OSTI ID: 1002354
• Journal Information: Acta Crystallogr. F, Vol. 66, Issue (4) ; 04, 2010
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE
HEME
HISTIDINE
NEUTRON DIFFRACTION
RESOLUTION
X-RAY DIFFRACTION
HORSES
METHEMOGLOBIN
CYANOGEN