9ZBV

Human TTR-C10A at pH 7.4

Summary for 9ZBV

• Entry DOI: 10.2210/pdb9zbv/pdb
• EMDB information: 74011
• Descriptor: Transthyretin (1 entity in total)
• Functional Keywords: thyroxine transporter, transport protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 4
• Total formula weight: 58821.49

Authors

Rafiq, M.,Schaefer, J.H.,Lander, G.C. (deposition date: 2025-11-21, release date: 2026-01-21, Last modification date: 2026-08-05)

Primary citation

Rafiq, M.,Schafer, J.H.,Rahmani, H.,You, S.,Bollong, M.,Grotjahn, D.,Wiseman, R.L.,Lander, G.C.
DM: a simple solution to suppress air-water interface interactions in cryo-EM.
Biorxiv, 2026

PubMed Abstract: The air-water interface (AWI) remains the primary barrier to routine high-resolution cryo-EM structure determination, driving protein adsorption, structural denaturation, and restricted particle orientations during vitrification. Here, we describe a simple and broadly applicable strategy to mitigate these effects using the mild non-ionic detergent n-decyl-β-D-maltopyranoside (DM). Addition of DM at low millimolar concentrations immediately prior to vitrification consistently suppresses AWI-driven artifacts, resulting in improved angular sampling, reduced structural damage, and enhanced reconstruction quality across diverse macromolecular systems. Using this approach, we obtained a high-resolution reconstruction of the 65 kDa Nucleophosmin 1 pentamer, a target previously limited by severe preferred orientation issues. We further show that DM promotes isotropic particle distributions for high-resolution reconstruction of hemagglutinin, transthyretin, as well as suppressing denaturation of aldolase while stabilizing its C-terminus. Our results indicate that DM effectively passivates deleterious air-water interface interactions without compromising particle integrity. These results establish DM as an effective additive for improving the robustness of single-particle cryo-EM sample preparation.

PubMed: 41959516
DOI: 10.64898/2026.04.02.716008

Experimental method

ELECTRON MICROSCOPY (3.2 Å)