Skip to content

After the revolution: how is Cryo-EM contributing to muscle research?

Research output: Contribution to journalArticle (Academic Journal)

Standard

After the revolution : how is Cryo-EM contributing to muscle research? / Bradshaw, Marston; Paul, Danielle M.

In: Journal of Muscle Research and Cell Motility, Vol. 40, No. 2, 13.07.2019, p. 93-98.

Research output: Contribution to journalArticle (Academic Journal)

Harvard

Bradshaw, M & Paul, DM 2019, 'After the revolution: how is Cryo-EM contributing to muscle research?', Journal of Muscle Research and Cell Motility, vol. 40, no. 2, pp. 93-98. https://doi.org/10.1007/s10974-019-09537-7

APA

Vancouver

Bradshaw M, Paul DM. After the revolution: how is Cryo-EM contributing to muscle research? Journal of Muscle Research and Cell Motility. 2019 Jul 13;40(2):93-98. https://doi.org/10.1007/s10974-019-09537-7

Author

Bradshaw, Marston ; Paul, Danielle M. / After the revolution : how is Cryo-EM contributing to muscle research?. In: Journal of Muscle Research and Cell Motility. 2019 ; Vol. 40, No. 2. pp. 93-98.

Bibtex

@article{00a5b75c31964900a3251ac73138ef0e,
title = "After the revolution: how is Cryo-EM contributing to muscle research?",
abstract = "The technique of electron microscopy (EM) has been fundamental to muscle research since the days of Huxley and Hanson. Direct observation of how proteins in the sarcomere are arranged and visualising the changes that occur upon activation have greatly increased our understanding of function. In the 1980s specimen preparation techniques for biological EM moved away from traditional fixing and staining. The technique known as cryo-electron microscopy (Cryo-EM) was developed, which involves rapidly freezing proteins in liquid ethane which maintains them in a near native state. Within the last 5 years there has been a step change in the achievable resolution using Cryo-EM. This {\textquoteleft}resolution revolution{\textquoteright} can be attributed to advances in detector technology, microscope automation and maximum likelihood image processing. In this article we look at how Cryo-EM has contributed to the field of muscle research in this post revolution era, focussing on recently published high resolution structures of sarcomeric proteins.",
keywords = "3D reconstruction, Actin, Cryo-EM, Myosin, Thin filament",
author = "Marston Bradshaw and Paul, {Danielle M.}",
year = "2019",
month = jul,
day = "13",
doi = "10.1007/s10974-019-09537-7",
language = "English",
volume = "40",
pages = "93--98",
journal = "Journal of Muscle Research and Cell Motility",
issn = "0142-4319",
publisher = "Springer Verlag",
number = "2",

}

RIS - suitable for import to EndNote

TY - JOUR

T1 - After the revolution

T2 - how is Cryo-EM contributing to muscle research?

AU - Bradshaw, Marston

AU - Paul, Danielle M.

PY - 2019/7/13

Y1 - 2019/7/13

N2 - The technique of electron microscopy (EM) has been fundamental to muscle research since the days of Huxley and Hanson. Direct observation of how proteins in the sarcomere are arranged and visualising the changes that occur upon activation have greatly increased our understanding of function. In the 1980s specimen preparation techniques for biological EM moved away from traditional fixing and staining. The technique known as cryo-electron microscopy (Cryo-EM) was developed, which involves rapidly freezing proteins in liquid ethane which maintains them in a near native state. Within the last 5 years there has been a step change in the achievable resolution using Cryo-EM. This ‘resolution revolution’ can be attributed to advances in detector technology, microscope automation and maximum likelihood image processing. In this article we look at how Cryo-EM has contributed to the field of muscle research in this post revolution era, focussing on recently published high resolution structures of sarcomeric proteins.

AB - The technique of electron microscopy (EM) has been fundamental to muscle research since the days of Huxley and Hanson. Direct observation of how proteins in the sarcomere are arranged and visualising the changes that occur upon activation have greatly increased our understanding of function. In the 1980s specimen preparation techniques for biological EM moved away from traditional fixing and staining. The technique known as cryo-electron microscopy (Cryo-EM) was developed, which involves rapidly freezing proteins in liquid ethane which maintains them in a near native state. Within the last 5 years there has been a step change in the achievable resolution using Cryo-EM. This ‘resolution revolution’ can be attributed to advances in detector technology, microscope automation and maximum likelihood image processing. In this article we look at how Cryo-EM has contributed to the field of muscle research in this post revolution era, focussing on recently published high resolution structures of sarcomeric proteins.

KW - 3D reconstruction

KW - Actin

KW - Cryo-EM

KW - Myosin

KW - Thin filament

UR - http://www.scopus.com/inward/record.url?scp=85068985460&partnerID=8YFLogxK

U2 - 10.1007/s10974-019-09537-7

DO - 10.1007/s10974-019-09537-7

M3 - Article (Academic Journal)

C2 - 31302812

AN - SCOPUS:85068985460

VL - 40

SP - 93

EP - 98

JO - Journal of Muscle Research and Cell Motility

JF - Journal of Muscle Research and Cell Motility

SN - 0142-4319

IS - 2

ER -