Cryo‐EM Resolves Molecular Recognition Of An Optojasp Photoswitch Bound To Actin Filaments In Both Switch States - Pospich - 2021 - Angewandte Chemie International Edition - Wiley Online Library
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Mechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides
![](https://i1.rgstatic.net/ii/profile.image/945783268462594-1602503711108_Q64/Florian-Kuellmer.jpg)
PDF) Cryo‐EM Resolves Molecular Recognition Of An Optojasp Photoswitch Bound To Actin Filaments In Both Switch States
![](https://www.researchgate.net/publication/354491348/figure/fig3/AS:1066309227933698@1631239339751/figure-supplement-2-Structural-variations-of-the-rigor-and-strong-ADP-states-of_Q320.jpg)
PDF) High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism
![](https://www.biorxiv.org/content/biorxiv/early/2020/08/25/2020.08.25.266262/F7.large.jpg)
Novel cryo-electron tomography structure of Arp2/3 complex in cells reveals mechanisms of branch formation
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Angewandte Chemie: Vol 133, No 16
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Cryo-EM Structures of the Actin:Tropomyosin Filament Reveal the Mechanism for the Transition from C- to M-State - ScienceDirect
![](https://www.pnas.org/cms/10.1073/pnas.1807028115/asset/6a5d8594-4995-4b7a-9881-5444aaed5379/assets/graphic/pnas.1807028115fig08.jpeg)
Mechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides
![](https://i1.rgstatic.net/publication/354491348_High-resolution_structures_of_the_actomyosin-V_complex_in_three_nucleotide_states_provide_insights_into_the_force_generation_mechanism/links/613abc8735e5e82234193d8f/largepreview.png)
PDF) High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism
![](https://www.pnas.org/cms/10.1073/pnas.1715836115/asset/436c1d54-c03b-4636-9661-e249ccf31afc/assets/graphic/pnas.1715836115fig03.jpeg)
Cryo-EM structure of the bacterial actin AlfA reveals unique assembly and ATP-binding interactions and the absence of a conserved subdomain
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Cryo‐EM Resolves Molecular Recognition Of An Optojasp Photoswitch Bound To Actin Filaments In Both Switch States - Pospich - 2021 - Angewandte Chemie International Edition - Wiley Online Library
![](https://iiif.elifesciences.org/lax/62514%2Felife-62514-fig3-v2.tif/full/1500,/0/default.jpg)
Molecular mechanism for direct actin force-sensing by α-catenin
![](https://www.researchgate.net/publication/368545838/figure/fig2/AS:11431281120518315@1676550135003/Cryo-EM-structure-of-the-SAM-bound-activated-state-CBS-a-Initial-representative-2D.png)
Cryo-EM structure of the SAM bound activated state CBS. a, Initial
![](https://www.biorxiv.org/content/biorxiv/early/2020/08/25/2020.08.25.266262/F5.large.jpg)
Novel cryo-electron tomography structure of Arp2/3 complex in cells reveals mechanisms of branch formation
![](https://www.thermofisher.com/bin/brightcove/image.jpeg?id=6340811739112&key=1964492303001)
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