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PDBsum entry 1l2k
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Oxygen storage/transport
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PDB id
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1l2k
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Hydrogen and deuterium in myoglobin as seen by a neutron structure determination at 1.5 a resolution.
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Authors
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A.Ostermann,
I.Tanaka,
N.Engler,
N.Niimura,
F.G.Parak.
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Ref.
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Biophys Chem, 2002,
95,
183-193.
[DOI no: ]
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PubMed id
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Abstract
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From the first days of protein neutron structure determination sperm whale
myoglobin was an object under investigation [Nature 224 (1969) 143, J. Mol.
Biol. 220 (1991) 381]. Nevertheless myoglobin is still of interest [Proc. Natl.
Acad. Sci. USA 97 (2000) 3872]. The feasibility of the monochromatic neutron
diffractometer BIX-3 at the JRR-3M reactor at the JAERI [J. Phys. Chem. Solids
60 (1999) 1623], to collect high-resolution diffraction data in a relatively
short time stimulated us to repeat the structural determination of myoglobin.
The structure of metmyoglobin has been determined up to a resolution of 1.5 A.
The hydrogen atoms were replaced in part, by deuterium soaking the crystals for
more than 10 years in D(2)O. A refinement of all atoms has been performed
including the refinement of individual mean square displacements and occupancies
of the exchangeable protons in backbone hydrogen bonds. A method is described to
show clear negative scattering densities of the H atoms. Water molecules within
the protein and on the molecule surface are shown. The exchangeability of H
atoms is correlated with structural distribution and flexibility.
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Secondary reference #1
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Title
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Neutrons expand the field of structural biology.
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Author
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N.Niimura.
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Ref.
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Curr Opin Struct Biol, 1999,
9,
602-608.
[DOI no: ]
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PubMed id
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