1rmv
From Proteopedia
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| - | [[Image:1rmv.gif|left|200px]] | + | [[Image:1rmv.gif|left|200px]] |
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| - | '''RIBGRASS MOSAIC VIRUS, FIBER DIFFRACTION''' | + | {{Structure |
| + | |PDB= 1rmv |SIZE=350|CAPTION= <scene name='initialview01'>1rmv</scene>, resolution 2.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''RIBGRASS MOSAIC VIRUS, FIBER DIFFRACTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RMV is a [ | + | 1RMV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Ribgrass_mosaic_virus Ribgrass mosaic virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RMV OCA]. |
==Reference== | ==Reference== | ||
| - | Molecular dynamics in refinement against fiber diffraction data., Wang H, Stubbs G, Acta Crystallogr A. 1993 May 1;49(3):504-13. PMID:[http:// | + | Molecular dynamics in refinement against fiber diffraction data., Wang H, Stubbs G, Acta Crystallogr A. 1993 May 1;49(3):504-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8129880 8129880] |
[[Category: Ribgrass mosaic virus]] | [[Category: Ribgrass mosaic virus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tobamovirus]] | [[Category: tobamovirus]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:53:47 2008'' |
Revision as of 11:53, 20 March 2008
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| , resolution 2.9Å | |||||||
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| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
RIBGRASS MOSAIC VIRUS, FIBER DIFFRACTION
Overview
The molecular dynamics (MD) method has been adapted for refinement of the structures of helical macromolecular aggregates aginst X-ray fiber diffraction data. To test the effectiveness of the method, refinements of the tobacco mosaic virus structure were carried out against a set of simulated fiber diffraction intensities using the MD method as well as the conventional restrained least-squares (RLS) method. The MD refinement converged to a very low R factor and produced a structure with generally satisfactory sterochemistry, while the RLS refinemnt was trapped at a local energy minimum with a larger R factor. Results suggest that the effective experimental radius of convergence of the MD method is significantly greater than that of the RLS method. Even when the initial structure is too far from the true structure to allow direct refinement, the MD method is able to find local minima that resemble the true structure sufficiently to allow improved phasing and thus lead to interpretable difference maps for model rebuilding.
About this Structure
1RMV is a Single protein structure of sequence from Ribgrass mosaic virus. Full crystallographic information is available from OCA.
Reference
Molecular dynamics in refinement against fiber diffraction data., Wang H, Stubbs G, Acta Crystallogr A. 1993 May 1;49(3):504-13. PMID:8129880
Page seeded by OCA on Thu Mar 20 13:53:47 2008
