EC Number   |
|---|
   3.6.4.B10 | cryo-EM structures of Saccharomyces cerevisiae TRiC in a nucleotide partially preloaded (NPP) state and in the ATP-bound state at 4.7 A and 4.6 A resolution, respectively |
| 3.6.4.B10 | cryo-specimen preparation of AML-1-ETO DNA-binding domain (AML1-175), with TRiC and Hsp70, and cryo-EM imaging, three-dimensional cryo-EM map reconstruction, modelling, method, overview. TRiC can refold denatured AML1-175 (DBD) and restore its DNA binding activity in vitro. Reconstructed the TRiC-AML1-175 complex forms in the presence of Ni2+-gold nanoparticles capable of binding to the His-tag on AML1-175. Ni-affinity nanogold particles reveal the location of AML1-175 on TRiC |
| 3.6.4.B10 | crystal structure analysis, PDB ID 3KFK |
| 3.6.4.B10 | crystal structure analysis, PDB ID 4D8Q |
| 3.6.4.B10 | crystal structure analysis, PDB IDs 3IYF and 3LOS, enzyme in open and closed state conformation |
| 3.6.4.B10 | homology model of the FAB1 apical domain and the top scoring model was with the 2.2 A resolution mouse CCTgamma apical domain template, PDB ID 1GML |
| 3.6.4.B10 | recombinant enzyme, removal of all surface exposed cysteine residues for diffracted X-ray tracking experiment, and addition of cysteine residues at the tip of helical protrusions of selected two subunits. Gold nanocrystals are attached onto CtCCTs via gold-thiol bonds and applied for the analysis by diffracted X-ray tracking |
| 3.6.4.B10 | structure analysis of the open conformation of the mammalian chaperonin CCT in complex with tubulin, overview |
