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FitEM2EM--tools for low resolution study of macromolecular assembly and dynamics.

Frankenstein Z, Sperling J, Sperling R, Eisenstein M - PLoS ONE (2008)

Bottom Line: The procedures incorporate thickening and smoothing of the surfaces of the objects which effectively compensates for differences in the resolution of the matched/docked objects, circumventing the need for resolution modification.The differences between the grid representations of the matched objects can be used to study conformation differences or to characterize the size and shape of substructures.The presented low-to-low docking tool FitEM2EMout ranked the expected models at the top.

View Article: PubMed Central - PubMed

Affiliation: Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.

ABSTRACT
Studies of the structure and dynamics of macromolecular assemblies often involve comparison of low resolution models obtained using different techniques such as electron microscopy or atomic force microscopy. We present new computational tools for comparing (matching) and docking of low resolution structures, based on shape complementarity. The matched or docked objects are represented by three dimensional grids where the value of each grid point depends on its position with regard to the interior, surface or exterior of the object. The grids are correlated using fast Fourier transformations producing either matches of related objects or docking models depending on the details of the grid representations. The procedures incorporate thickening and smoothing of the surfaces of the objects which effectively compensates for differences in the resolution of the matched/docked objects, circumventing the need for resolution modification. The presented matching tool FitEM2EMin successfully fitted electron microscopy structures obtained at different resolutions, different conformers of the same structure and partial structures, ranking correct matches at the top in every case. The differences between the grid representations of the matched objects can be used to study conformation differences or to characterize the size and shape of substructures. The presented low-to-low docking tool FitEM2EMout ranked the expected models at the top.

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Related in: MedlinePlus

The dependency of the optimal w values on the resolution of the matched EM maps.The full circles depict the results of self-matching (for systems listed in Table 1). The hollow circles depict the results of matching of related EM maps (the average resolution is used here). The regression line (y = −0.0612x+3.7551; R2 = 0.78) is based only on the full circles. The error bars reflect the range of the optimal w.
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pone-0003594-g001: The dependency of the optimal w values on the resolution of the matched EM maps.The full circles depict the results of self-matching (for systems listed in Table 1). The hollow circles depict the results of matching of related EM maps (the average resolution is used here). The regression line (y = −0.0612x+3.7551; R2 = 0.78) is based only on the full circles. The error bars reflect the range of the optimal w.

Mentions: R2 is the virtual atoms radius calculated with w values derived from the linear dependency of w on the resolution (Figure 1).


FitEM2EM--tools for low resolution study of macromolecular assembly and dynamics.

Frankenstein Z, Sperling J, Sperling R, Eisenstein M - PLoS ONE (2008)

The dependency of the optimal w values on the resolution of the matched EM maps.The full circles depict the results of self-matching (for systems listed in Table 1). The hollow circles depict the results of matching of related EM maps (the average resolution is used here). The regression line (y = −0.0612x+3.7551; R2 = 0.78) is based only on the full circles. The error bars reflect the range of the optimal w.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2572833&req=5

pone-0003594-g001: The dependency of the optimal w values on the resolution of the matched EM maps.The full circles depict the results of self-matching (for systems listed in Table 1). The hollow circles depict the results of matching of related EM maps (the average resolution is used here). The regression line (y = −0.0612x+3.7551; R2 = 0.78) is based only on the full circles. The error bars reflect the range of the optimal w.
Mentions: R2 is the virtual atoms radius calculated with w values derived from the linear dependency of w on the resolution (Figure 1).

Bottom Line: The procedures incorporate thickening and smoothing of the surfaces of the objects which effectively compensates for differences in the resolution of the matched/docked objects, circumventing the need for resolution modification.The differences between the grid representations of the matched objects can be used to study conformation differences or to characterize the size and shape of substructures.The presented low-to-low docking tool FitEM2EMout ranked the expected models at the top.

View Article: PubMed Central - PubMed

Affiliation: Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.

ABSTRACT
Studies of the structure and dynamics of macromolecular assemblies often involve comparison of low resolution models obtained using different techniques such as electron microscopy or atomic force microscopy. We present new computational tools for comparing (matching) and docking of low resolution structures, based on shape complementarity. The matched or docked objects are represented by three dimensional grids where the value of each grid point depends on its position with regard to the interior, surface or exterior of the object. The grids are correlated using fast Fourier transformations producing either matches of related objects or docking models depending on the details of the grid representations. The procedures incorporate thickening and smoothing of the surfaces of the objects which effectively compensates for differences in the resolution of the matched/docked objects, circumventing the need for resolution modification. The presented matching tool FitEM2EMin successfully fitted electron microscopy structures obtained at different resolutions, different conformers of the same structure and partial structures, ranking correct matches at the top in every case. The differences between the grid representations of the matched objects can be used to study conformation differences or to characterize the size and shape of substructures. The presented low-to-low docking tool FitEM2EMout ranked the expected models at the top.

Show MeSH
Related in: MedlinePlus