Membrane mimetic systems in CryoEM: keeping membrane proteins in their native environment

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Standard

Membrane mimetic systems in CryoEM : keeping membrane proteins in their native environment. / Autzen, Henriette E.; Julius, David; Cheng, Yifan.

In: Current Opinion in Structural Biology, Vol. 58, 10.2019, p. 259-268.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperReviewResearchpeer-review

Harvard

Autzen, HE, Julius, D & Cheng, Y 2019, 'Membrane mimetic systems in CryoEM: keeping membrane proteins in their native environment', Current Opinion in Structural Biology, vol. 58, pp. 259-268. https://doi.org/10.1016/j.sbi.2019.05.022

APA

Autzen, H. E., Julius, D., & Cheng, Y. (2019). Membrane mimetic systems in CryoEM: keeping membrane proteins in their native environment. Current Opinion in Structural Biology, 58, 259-268. https://doi.org/10.1016/j.sbi.2019.05.022

CBE

Autzen HE, Julius D, Cheng Y. 2019. Membrane mimetic systems in CryoEM: keeping membrane proteins in their native environment. Current Opinion in Structural Biology. 58:259-268. https://doi.org/10.1016/j.sbi.2019.05.022

MLA

Autzen, Henriette E., David Julius and Yifan Cheng. "Membrane mimetic systems in CryoEM: keeping membrane proteins in their native environment". Current Opinion in Structural Biology. 2019, 58. 259-268. https://doi.org/10.1016/j.sbi.2019.05.022

Vancouver

Autzen HE, Julius D, Cheng Y. Membrane mimetic systems in CryoEM: keeping membrane proteins in their native environment. Current Opinion in Structural Biology. 2019 Oct;58:259-268. https://doi.org/10.1016/j.sbi.2019.05.022

Author

Autzen, Henriette E. ; Julius, David ; Cheng, Yifan. / Membrane mimetic systems in CryoEM : keeping membrane proteins in their native environment. In: Current Opinion in Structural Biology. 2019 ; Vol. 58. pp. 259-268.

Bibtex

@article{161e6fbfbc9f4068b6bc93adf57121a6,
title = "Membrane mimetic systems in CryoEM: keeping membrane proteins in their native environment",
abstract = "Advances in electron microscopes, detectors and data processing algorithms have greatly facilitated the structural determination of many challenging integral membrane proteins that have been evasive to crystallization. These breakthroughs facilitate the application and development of various membrane protein solubilization approaches for structural studies, including reconstitution into lipid nanoparticles. In this review, we discuss various approaches for preparing transmembrane proteins for structural determination with single-particle electron cryo microscopy (cryoEM).",
author = "Autzen, {Henriette E.} and David Julius and Yifan Cheng",
year = "2019",
month = oct,
doi = "10.1016/j.sbi.2019.05.022",
language = "English",
volume = "58",
pages = "259--268",
journal = "Current Opinion in Structural Biology",
issn = "0959-440X",
publisher = "Elsevier Ltd. * Current Opinion Journals",

}

RIS

TY - JOUR

T1 - Membrane mimetic systems in CryoEM

T2 - keeping membrane proteins in their native environment

AU - Autzen, Henriette E.

AU - Julius, David

AU - Cheng, Yifan

PY - 2019/10

Y1 - 2019/10

N2 - Advances in electron microscopes, detectors and data processing algorithms have greatly facilitated the structural determination of many challenging integral membrane proteins that have been evasive to crystallization. These breakthroughs facilitate the application and development of various membrane protein solubilization approaches for structural studies, including reconstitution into lipid nanoparticles. In this review, we discuss various approaches for preparing transmembrane proteins for structural determination with single-particle electron cryo microscopy (cryoEM).

AB - Advances in electron microscopes, detectors and data processing algorithms have greatly facilitated the structural determination of many challenging integral membrane proteins that have been evasive to crystallization. These breakthroughs facilitate the application and development of various membrane protein solubilization approaches for structural studies, including reconstitution into lipid nanoparticles. In this review, we discuss various approaches for preparing transmembrane proteins for structural determination with single-particle electron cryo microscopy (cryoEM).

UR - http://www.scopus.com/inward/record.url?scp=85068250429&partnerID=8YFLogxK

U2 - 10.1016/j.sbi.2019.05.022

DO - 10.1016/j.sbi.2019.05.022

M3 - Review

C2 - 31279500

AN - SCOPUS:85068250429

VL - 58

SP - 259

EP - 268

JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

SN - 0959-440X

ER -