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Hemocyanins are responsible for transporting O 2 in the arthropod and molluscan hemolymph. Haliotis diversicolor molluscan hemocyanin isoform 1 (HdH1) is an 8 MDa oligomer. Each subunit is made up of eight functional units (FUs). Each FU contains two Cu ions, which can reversibly bind an oxygen molecule. Here, we report a 4.5 Å cryo-EM structure of HdH1. The structure clearly shows ten asymmetric units...
In this work, we employ single-particle electron cryo-microscopy (cryo-EM) to reconstruct GroEL to ∼4 Å resolution with both D7 and C7 symmetry. Using a newly developed skeletonization algorithm and secondary structure element identification in combination with sequence-based secondary structure prediction, we demonstrate that it is possible to achieve a de novo Cα trace directly from a cryo-EM reconstruction...
Electron cryomicroscopy reveals an unprecedented conformation of the single-ring mutant of GroEL (SR398) bound to GroES in the presence of Mg-ATP. This conformation exhibits a considerable expansion of the folding cavity, with ∼80% more volume than the X-ray structure of the equivalent cis cavity in the GroEL-GroES-(ADP) 7 complex. This expanded conformation can encapsulate an 86 kDa heterodimeric...
We present a reconstruction of native GroEL by electron cryomicroscopy (cryo-EM) and single particle analysis at 6 Å resolution. α helices are clearly visible and β sheet density is also visible at this resolution. While the overall conformation of this structure is quite consistent with the published X-ray data, a measurable shift in the positions of three α helices in the intermediate domain is...
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