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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.

SUBMITTER: Kovalevsky AY

PROVIDER: S-EPMC2852348 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature

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Preliminary neutron and X-ray crystallographic studies of equine cyanomethemoglobin.

Kovalevsky A Y AY Fisher S Zoe SZ Seaver Sean S Mustyakimov Marat M Sukumar Narayanasami N Langan Paul P Mueser Timothy C TC Hanson B Leif BL

Acta crystallographica. Section F, Structural biology and crystallization communications 20100331 Pt 4

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. In ...[more]

PMID: 20383026

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