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Article

High-Resolution Cryo-Electron Microscopy Structure Determination of Haemophilus influenzae Tellurite-Resistance Protein A via 200 kV Transmission Electron Microscopy

by
Nhi L. Tran
†,
Skerdi Senko
†,
Kyle W. Lucier
,
Ashlyn C. Farwell
,
Sabrina M. Silva
,
Phat V. Dip
,
Nicole Poweleit
,
Giovanna Scapin
and
Claudio Catalano
*
NanoImaging Services, 4940 Carroll Canyon Road, Suite 115, San Diego, CA 92121, USA
*
Author to whom correspondence should be addressed.
†
These authors contributed equally to this work.
Int. J. Mol. Sci. 2024, 25(8), 4528; https://doi.org/10.3390/ijms25084528
Submission received: 29 March 2024 / Revised: 16 April 2024 / Accepted: 18 April 2024 / Published: 20 April 2024
(This article belongs to the Special Issue Cryogenic Biomolecular Imaging and Image Analysis Techniques: Present and Future)
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Abstract

Membrane proteins constitute about 20% of the human proteome and play crucial roles in cellular functions. However, a complete understanding of their structure and function is limited by their hydrophobic nature, which poses significant challenges in purification and stabilization. Detergents, essential in the isolation process, risk destabilizing or altering the proteins’ native conformations, thus affecting stability and functionality. This study leverages single-particle cryo-electron microscopy to elucidate the structural nuances of membrane proteins, focusing on the SLAC1 bacterial homolog from Haemophilus influenzae (HiTehA) purified with diverse detergents, including n-dodecyl β-D-maltopyranoside (DDM), glycodiosgenin (GDN), β-D-octyl-glucoside (OG), and lauryl maltose neopentyl glycol (LMNG). This research not only contributes to the understanding of membrane protein structures but also addresses detergent effects on protein purification. By showcasing that the overall structural integrity of the channel is preserved, our study underscores the intricate interplay between proteins and detergents, offering insightful implications for drug design and membrane biology.
Keywords: cryo-EM; 200 kV; membrane protein; fully embed; alpha-helical; detergents; structural biology cryo-EM; 200 kV; membrane protein; fully embed; alpha-helical; detergents; structural biology

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MDPI and ACS Style

Tran, N.L.; Senko, S.; Lucier, K.W.; Farwell, A.C.; Silva, S.M.; Dip, P.V.; Poweleit, N.; Scapin, G.; Catalano, C. High-Resolution Cryo-Electron Microscopy Structure Determination of Haemophilus influenzae Tellurite-Resistance Protein A via 200 kV Transmission Electron Microscopy. Int. J. Mol. Sci. 2024, 25, 4528. https://doi.org/10.3390/ijms25084528

AMA Style

Tran NL, Senko S, Lucier KW, Farwell AC, Silva SM, Dip PV, Poweleit N, Scapin G, Catalano C. High-Resolution Cryo-Electron Microscopy Structure Determination of Haemophilus influenzae Tellurite-Resistance Protein A via 200 kV Transmission Electron Microscopy. International Journal of Molecular Sciences. 2024; 25(8):4528. https://doi.org/10.3390/ijms25084528

Chicago/Turabian Style

Tran, Nhi L., Skerdi Senko, Kyle W. Lucier, Ashlyn C. Farwell, Sabrina M. Silva, Phat V. Dip, Nicole Poweleit, Giovanna Scapin, and Claudio Catalano. 2024. "High-Resolution Cryo-Electron Microscopy Structure Determination of Haemophilus influenzae Tellurite-Resistance Protein A via 200 kV Transmission Electron Microscopy" International Journal of Molecular Sciences 25, no. 8: 4528. https://doi.org/10.3390/ijms25084528

APA Style

Tran, N. L., Senko, S., Lucier, K. W., Farwell, A. C., Silva, S. M., Dip, P. V., Poweleit, N., Scapin, G., & Catalano, C. (2024). High-Resolution Cryo-Electron Microscopy Structure Determination of Haemophilus influenzae Tellurite-Resistance Protein A via 200 kV Transmission Electron Microscopy. International Journal of Molecular Sciences, 25(8), 4528. https://doi.org/10.3390/ijms25084528

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