2026· Methods in molecular biology· Vol 3070, pp.
263-282
· 0 citations
Medicine
TL;DR
This study investigates the eukaryotic chaperonin CCT, a ~1 MDa hetero-oligomeric complex essential for the folding of key substrates such as actin, tubulin, and WD40 family members and demonstrates that subunit assignment and atomic modeling are achievable by exploiting subunit-intrinsic structural features alone.
Cryogenic electron microscopy (cryo-EM) has enabled rapid progress in structural biology throughout the last decade. However, cryo-EM sample preparation still represents a major bottleneck in high-resolution structure determination. Many proteins and macromolecular complexes interact with the air-water interface during...
Rose Young, Amy J. S. McGeoch, M. Jessop et al.· bioRxiv· 0 citations
This review highlights the range of resolutions and cellular structures accessible by cryo-ET, and the kinds of biological insights that may be obtained, using eukaryotic parasites as case studies, and combines with orthogonal techniques.
Nicolas Coudray, Damian C. Ekiert, G. Bhabha· Current Opinion in Structura...· 0 citations
Structural determination of small membrane proteins by cryo-electron microscopy (cryo-EM) remains inherently challenging due to their low molecular weight, conformational heterogeneity, and lack of prominent structural features for reliable particle alignment. In this chapter, we describe how to design and perform biop...
Amrutha H. Chidananda, Camilo Perez· Methods in molecular biology· 0 citations
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