VitisC: Visualizing interested target via integrated scaffold of cytoophidium
Yin, B.; Hu, H.-H.; Zhong, J.; Liu, J.-L.
Show abstract
Cryo-electron microscopy (cryo-EM) single-particle analysis has become a widely used technique for high-resolution structural determination of biological macromolecules and complexes. However, the determination of the structure of small molecule proteins remains a limitation of this technology. To address this issue, here we develop a novel approach termed Visualizing interested target via integrated scaffold of cytoophidium (VitisC). We use a filamentous structure formed by Escherichia coli CTP synthase (CTPS) as the scaffold, termed the scaffold of cytoophidium. Through artificial design and modification, small proteins can be attached to this symmetrical scaffold, which is very suitable for cryo-EM imaging. The formation conditions for stable filament structures of the fusion protein are optimized in vitro, and the three-dimensional structure of the fusion protein is reconstructed using cryo-EM single-particle analysis, achieving an overall resolution of 3.39 [A]. Therefore, cryo-EM is successfully applied to visualize small proteins. VitisC not only demonstrates the feasibility of employing cytoophidia as scaffolds, but also provides an approach for high-resolution structural analysis of small proteins using Cryo-EM.
Matching journals
The top 6 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Amino and PEG-Amino Graphene Oxide Grids Enrich and Protect Samples for High-resolution Single Particle Cryo-electron Microscopy 95%
- Ice thickness control and measurement in the VitroJet for time-efficient single particle structure determination 95%
- Cryo-EM reveals the structure and dynamics of a 723-residue malate synthase G 94%
Similar papers in this journal
- CASSPER: A Semantic Segmentation based Particle Picking Algorithm for Single Particle Cryo-Electron Microscopy 94%
- cryoTIGER: Deep-Learning Based Tilt Interpolation Generator for Enhanced Reconstruction in Cryo Electron Tomography 94%
- Cryo-electron tomography of cardiac myofibrils reveals a contraction-induced lattice twist in the Z-discs. 94%
Similar papers in this journal
- DomainFit: Identification of Protein Domains in cryo-EM maps at Intermediate Resolution using AlphaFold2-predicted Models 94%
- CryoVIA - An image analysis toolkit for the quantification of membrane structures from cryo-EM micrographs 94%
- Cost-benefit analysis of cryogenic electron tomography subtomogram averaging of chaperonin MmCpn at near atomic resolution. 94%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.