1iob: Difference between revisions
New page: left|200px<br /> <applet load="1iob" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iob, resolution 2.0Å" /> '''INTERLEUKIN-1 BETA F... |
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[[Image:1iob.gif|left|200px]]<br /> | [[Image:1iob.gif|left|200px]]<br /><applet load="1iob" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1iob, resolution 2.0Å" /> | caption="1iob, resolution 2.0Å" /> | ||
'''INTERLEUKIN-1 BETA FROM JOINT X-RAY AND NMR REFINEMENT'''<br /> | '''INTERLEUKIN-1 BETA FROM JOINT X-RAY AND NMR REFINEMENT'''<br /> | ||
==Overview== | ==Overview== | ||
Joint refinement of macromolecules against crystallographic and nuclear | Joint refinement of macromolecules against crystallographic and nuclear magnetic resonance (NMR) observations is presented as a way of combining experimental information from the two methods. The model of interleukin-1 beta derived by the joint x-ray and NMR refinement is shown to be consistent with the experimental observations of both methods and to have crystallographic R value and geometrical parameters that are of the same quality as or better than those of models obtained by conventional crystallographic studies. The few NMR observations that are violated by the model serve as an indicator for genuine differences between the crystal and solution structures. The joint x-ray-NMR refinement can resolve structural ambiguities encountered in studies of multidomain proteins, in which low- to medium-resolution diffraction data can be complemented by higher resolution NMR data obtained for the individual domains. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1IOB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1IOB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IOB OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Clore, G | [[Category: Clore, G M.]] | ||
[[Category: Shaanan, B.]] | [[Category: Shaanan, B.]] | ||
[[Category: cytokine]] | [[Category: cytokine]] | ||
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[[Category: pyrogen]] | [[Category: pyrogen]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:53 2008'' | ||
Revision as of 14:14, 21 February 2008
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INTERLEUKIN-1 BETA FROM JOINT X-RAY AND NMR REFINEMENT
OverviewOverview
Joint refinement of macromolecules against crystallographic and nuclear magnetic resonance (NMR) observations is presented as a way of combining experimental information from the two methods. The model of interleukin-1 beta derived by the joint x-ray and NMR refinement is shown to be consistent with the experimental observations of both methods and to have crystallographic R value and geometrical parameters that are of the same quality as or better than those of models obtained by conventional crystallographic studies. The few NMR observations that are violated by the model serve as an indicator for genuine differences between the crystal and solution structures. The joint x-ray-NMR refinement can resolve structural ambiguities encountered in studies of multidomain proteins, in which low- to medium-resolution diffraction data can be complemented by higher resolution NMR data obtained for the individual domains.
DiseaseDisease
Known disease associated with this structure: Gastric cancer risk after H. pylori infection OMIM:[147720]
About this StructureAbout this Structure
1IOB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Combining experimental information from crystal and solution studies: joint X-ray and NMR refinement., Shaanan B, Gronenborn AM, Cohen GH, Gilliland GL, Veerapandian B, Davies DR, Clore GM, Science. 1992 Aug 14;257(5072):961-4. PMID:1502561
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