Preliminary neutron and X-ray crystallographic studies of equine cyanomethemoglobin

A. Y. Kovalevsky; S. Zoe Fisher; Sean Seaver; Marat Mustyakimov; Narayanasami Sukumar; Paul Langan; Timothy C. Mueser; B. Leif Hanson

doi:10.1107/S1744309110007840

Preliminary neutron and X-ray crystallographic studies of equine cyanomethemoglobin

A. Y. Kovalevsky, S. Zoe Fisher, Sean Seaver, Marat Mustyakimov, Narayanasami Sukumar, Paul Langan, Timothy C. Mueser, B. Leif Hanson

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	474-477
Number of pages	4
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	66
Issue number	4
DOIs	https://doi.org/10.1107/S1744309110007840
State	Published - 2010
Externally published	Yes

Keywords

Equine hemoglobin
Joint XN refinement
Protonation
R state
Time-of-flight neutron diffraction

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10.1107/S1744309110007840

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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}",

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language = "English",

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pages = "474--477",

journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

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TY - JOUR

T1 - Preliminary neutron and X-ray crystallographic studies of equine cyanomethemoglobin

AU - Kovalevsky, A. Y.

AU - Fisher, S. Zoe

AU - Seaver, Sean

AU - Mustyakimov, Marat

AU - Sukumar, Narayanasami

AU - Langan, Paul

AU - Mueser, Timothy C.

AU - Hanson, B. Leif

PY - 2010

Y1 - 2010

N2 - 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.

AB - 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.

KW - Equine hemoglobin

KW - Joint XN refinement

KW - Protonation

KW - R state

KW - Time-of-flight neutron diffraction

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JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

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Preliminary neutron and X-ray crystallographic studies of equine cyanomethemoglobin

Abstract

Keywords

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