Intermediate filament protein structure determination.

摘要: Publisher Summary X-ray crystallography is one of the few experimental methods that makes possible to study intermediate filament (IF) structure at atomic resolution; however, prerequisite for a crystallographic analysis ability produce macroscopic, well-ordered crystals. This chapter focuses on existing experience with x-ray crystallography. It also discusses another diffraction method—small angle scattering (SAXS)–which used investigate IF higher assembly levels than dimer. outlines approaches bring together data protein obtained by various methods, aiming constructing three-dimensional model complete IFs—a goal has not been achieved yet. Although, structural resolution provided SAXS less crystallography, advantage it works solutions and, hence, does depend availability Moreover, allows monitoring consequent steps varying solution conditions and provides additional information pathway. The crystallization stable complexes formed fragments difficult task; this should provide essential detail four dimer–dimer contact types occurring in mature IFs. Both have large future potential toward getting more insight into interactions elementary dimers during assembly.