Jiu Li Song

TL;DR: A reconstruction of native GroEL by electron cryomicroscopy (cryo-EM) and single particle analysis at 6 A resolution and a measurable shift in the positions of three alpha helices in the intermediate domain is observed, not consistent with any of the 7 monomeric structures in the Protein Data Bank model (1OEL).

TL;DR: It is demonstrated that it is possible to achieve a de novo Calpha trace directly from a cryo-EM reconstruction of GroEL, and the topology of the backbone trace is completely accurate, though subtle alterations illustrate significant differences from existing crystal structures.

TL;DR: This work presents a three-dimensional reconstruction of native naked GroEL to approximately 11.5 A performed entirely with EMAN, and demonstrates that the single-particle reconstruction,X-ray scattering data and X-ray crystal structure all agree well at this resolution.

TL;DR: Electron cryomicroscopy reveals an unprecedented conformation of the single-ring mutant of GroEL (SR398) bound to GroES in the presence of Mg-ATP, which can encapsulate an 86 kDa heterodimeric (alphabeta) assembly intermediate of mitochondrial branched-chain alpha-ketoacid dehydrogenase, the largest substrate ever observed to be cis encapsulated.

TL;DR: It is proposed that the augmented E1 activity is responsible for robust thiamin responsiveness in homozygous patients carrying the H391R E2 mutation and that the presence of a full-length mutant E2 is diagnostic of this MSUD phenotype.