Protein domain mapping by internal labeling and single particle electron microscopy.

ABSTRACT: In recent years, electron microscopy (EM) and single particle analysis have emerged as essential tools for investigating the architecture of large biological complexes. When high resolution is achievable, crystal structure docking and de-novo modeling allows for precise assignment of individual protein domain sequences. However, the achievable resolution may limit the ability to do so, especially when small or flexible complexes are under study. In such cases, protein labeling has emerged as an important complementary tool to characterize domain architecture and elucidate functional mechanistic details. All labeling strategies proposed to date are either focused on the identification of the position of protein termini or require multi-step labeling strategies, potentially interfering with

SUBMITTER: Ciferri C 

PROVIDER: S-EPMC4921062 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature