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ABSTRACT: Background
The number of available structures of large multi-protein assemblies is quite small. Such structures provide phenomenal insights on the organization, mechanism of formation and functional properties of the assembly. Hence detailed analysis of such structures is highly rewarding. However, the common problem in such analyses is the low resolution of these structures. In the recent times a number of attempts that combine low resolution cryo-EM data with higher resolution structures determined using X-ray analysis or NMR or generated using comparative modeling have been reported. Even in such attempts the best result one arrives at is the very course idea about the assembly structure in terms of trace of the C(alpha) atoms which are modeled with modest accuracy.Methodolo
SUBMITTER: Gadkari RA
PROVIDER: S-EPMC2641018 | biostudies-literature | 2009
REPOSITORIES: biostudies-literature