1l2k: Difference between revisions

Revision as of 14:40, 21 February 2008

Neutron Structure Determination of Sperm Whale Met-Myoglobin at 1.5A Resolution.

OverviewOverview

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.

About this StructureAbout this Structure

1L2K is a Single protein structure of sequence from Physeter catodon with , , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Hydrogen and deuterium in myoglobin as seen by a neutron structure determination at 1.5 A resolution., Ostermann A, Tanaka I, Engler N, Niimura N, Parak FG, Biophys Chem. 2002 Mar 28;95(3):183-93. PMID:12062378

Page seeded by OCA on Thu Feb 21 13:40:35 2008

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OCA

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-[[Image:1l2k.gif|left|200px]]<br /><applet load="1l2k" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1l2k.gif|left|200px]]<br /><applet load="1l2k" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1l2k, resolution 1.50&Aring;" />
 '''Neutron Structure Determination of Sperm Whale Met-Myoglobin at 1.5A Resolution.'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-L2K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with SO4, ND4, HEM and DOD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L2K OCA].
+L2K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ND4:'>ND4</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=DOD:'>DOD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2K OCA].
 ==Reference==
@@ Line 16: / Line 16: @@
 [[Category: Niimura, N.]]
 [[Category: Ostermann, A.]]
-[[Category: Parak, F.G.]]
+[[Category: Parak, F G.]]
 [[Category: Tanaka, I.]]
 [[Category: DOD]]
@@ Line 27: / Line 27: @@
 [[Category: neutron structure]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:11:28 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:35 2008''