• William Kahn posted an update 2 months ago

    The crystal was inside the space group H3 with eight polypeptides (designated as A to H) inside the asymmetric unit. The threefold crystallographic symmetry operated on the asymmetric unit content material to create a 24-mer cage. The packing with the Hpf-E2 subunits inside the nanocage structure was identical to that in the Hpf-E1, with minor…[Read more]

  • The crystal was in the space group H3 with eight polypeptides (designated as A to H) in the asymmetric unit. The threefold crystallographic symmetry operated around the asymmetric unit content to create a 24-mer cage. The packing on the Hpf-E2 subunits within the nanocage structure was identical to that from the Hpf-E1, with minor shifts in…[Read more]

  • The packing from the Hpf-E2 subunits inside the nanocage structure was identical to that of your Hpf-E1, with minor shifts in relative positions (see alignments of subunits beneath for particulars). As a result of the fairly low resolution, only 11 water molecules and no other ions/small molecules had been modeled (Table 1). The Hpf-E2 protein was…[Read more]

  • Tallographic fourfold Rate of TRPM7-deficient HAP1 cells was considerably reduced when compared symmetry to create a 24-mer spherical cage. By aligning one particular subunit, the Ca traces of all subunits of your two cages superposed completely. The crystals had been grown inside the presence of 1.6 M NaCl and 20 glycerol, and at the very least…[Read more]

  • Tallographic fourfold symmetry to generate a 24-mer spherical cage. Each cage includes a total solvent-accessible surface region of 148 000 A2 and a total location buried in the inter-subunit interfaces of 74 000 A2. The two cages had identical packing in the subunits. By aligning one subunit, the Ca traces of all subunits of the two cages…[Read more]

  • Load More