Crystallography supplies unparalleled detail on structural information critical for mechanistic
analyses; however, it is restricted to describing low energy conformations of …

Various types of large-amplitude molecular deformation are ubiquitously involved in the
functions of biological macromolecules, especially supramolecular complexes. They can be …

Structures of macromolecular complexes are necessary for a mechanistic description of
biochemical and cellular processes. They can be solved by experimental methods, such as …

The pyruvate dehydrogenase complex (PDHc) is a key megaenzyme linking glycolysis with
the citric acid cycle. In mammalian PDHc, dihydrolipoamide acetyltransferase (E2) and the …

p97/VCP is a member of the AAA ATPase family and has roles in both membrane fusion and
ubiquitin dependent protein degradation. Here, we present a 3.6 Å crystal structure of …

The deformation patterns of a large set of representative proteins determined by essential
dynamics extracted from atomistic simulations and coarse-grained normal mode analysis …

We suggest a simple method to assess how many normal modes are needed to map a
conformational change. By projecting the conformational change onto a subspace of the …

We examined the role of molecular shape in determining the patterns of low-frequency
deformational motions of biological macromolecules. The low-frequency subspace of …

The subunits of the dihydrolipoyl acetyltransferase (E2) component of mammalian pyruvate
dehydrogenase complex can form a 60-mer via association of the C-terminal I domain of E2 …

Dihydrolipoyl acetyltransferase (E2) is the central component of pyruvate dehydrogenase
complex (PDC), which converts pyruvate to acetyl-CoA. Structural comparison by cryo …