Abrin is a macromolecular complex consisting of two protein subunits termed A and B.

The human SMN protein is part of a large macromolecular complex involved in the biogenesis of small ribonucleoproteins.

RyRs are massive structures comprising the largest known ion channel-bearing macromolecular complex and exceeding 3 million Daltons in molecular weight.

The type II secretion system (T2SS) is a macromolecular complex spanning the inner and outer membranes of Gram-negative bacteria.

The tests include the cases where a macromolecular complex exhibits structural flexibility and cases where a molecule is found in ligand-bound and unbound states.

The cytoskeletal proteins talin and vinculin form part of a macromolecular complex on the cytoplasmic face of integrin-mediated cellular junctions with the extracellular matrix.

Epithelial junction formation and maintenance are multistep processes that rely on the clustering of macromolecular complexes.

Instead, it forms macromolecular complexes that have been reported to exert both positive and negative modes of regulation.

Targeting and transporting these proteins to the flagella are simplified by preassembly of macromolecular complexes in the cell body.

Given recent progress, native MS is anticipated to play an increasingly important role for researchers interested in the structure of macromolecular complexes.

This is particularly significant in the case of macromolecular complexes where intermolecular translational restraints derived from nuclear Overhauser enhancement data may be limited.

Recently, ET has reached sub-nanometer resolution for investigating the native and conformational dynamics of macromolecular complexes by combining with the sub-tomogram averaging approach.

Recent studies have demonstrated that RyR are macromolecular complexes comprising of 4 pore-forming channel subunits, each of which is associated with regulatory subunits.

It can reveal the stoichiometry of subunits as well as their two-dimensional interaction network and provide information regarding the dynamic behavior of macromolecular complexes.

The goal of time-resolved cryo-electron microscopy is to determine structural models for transient functional states of large macromolecular complexes such as ribosomes and viruses.