(Supplementary Fig.6c) thus influencing the P5.50I3.40F6.44motif, which was found in many GPCRs as an allosteric bridge to coordinate the communications between the ligand-binding pockets and G protein-coupling interfaces47. It was suggested that the translocation of F6.44in the PIF motif ...
Cryo-EM reveals that the peptide inserts in loop128-131 of αHL do not interfere with the formation of the heptameric pore structure To further verify that inserts in loop128-131 of αHL do not interfere with pore formation and membrane insertion, we collected structural data using cryo-EM....
3). Some of the selected targeting regions overlap with the native interfaces, but no native interface information or native hotspots were used during the binder design process. For some targets (for example, CD3δ and VirB8), no structures of the native complex were available and there were ...
We report the capsid structure of the African cichlid nackednavirus (ACNDV), determined by cryo-EM at 3.7 Å resolution. This enables direct comparison with the known capsid structures of HBV and duck HBV, prototypic representatives of the mammalian and avian lineages of the enveloped Hepa...
The blue and red boxes indicate the interaction interfaces between AcrVA1 and LbCas12a. (D) Close-up view of crRNA and AcrVA1. Cryo-EM density is shown in mesh. Shown below is a schematic of the crRNA used in this study, with disordered segment shown in a gray background. (E) ...
cryo-electron microscopy (cryoEM) and dynamic light scattering (DLS; Fig.1c,d), and removal of MβCD by the detection of residual sugar (Supplementary Fig.1andMethods). The ability of MβCD to mediate exchange between the DMPC and DMPG lipids was confirmed using the fluorescent marker ...
Modeling flexible macromolecules is one of the foremost challenges in single-particle cryogenic-electron microscopy (cryo-EM), with the potential to illuminate fundamental questions in structural biology. We introduce Three-Dimensional Flexible Refinemen
Fig. 1: Cryo-EM map of the human GPI-T. aGPI-T replaces the C-terminal signal peptide (CSP) of proproteins with GPI at the ω residue (blue) by a transamination reaction. Various parts are denoted in the dashed box. EtNP, ethanolamine phosphate; Man, mannose; Ino, inositol; GlcNH2...
Structural details of MFAP4 and its potential interfaces for these interactions are unknown. Here, we present a cryo-electron microscopy structure of human MFAP4. In the presence of calcium, MFAP4 assembles as an octamer, where two sets of homodimers constitute the top and bottom halves of ...
Cryo-TEM imaging of the proteins in their native state (Fig. 5a,b Insets) and AFM that relies on protein interaction with the Highly Ordered Pyrolytic Graphic (HOPG) substrate (Fig. 5d–f) validate the globular nature of aggregates. Because SCPPPQ1 requires urea to be solubilized and...