1S-B2-2In Situ Structural Studies of Macro Molecular Complexes in Cells by Cryo-electron Tomography with Volta Phase Plate

Microscopy ◽  
2017 ◽  
Vol 66 (suppl_1) ◽  
pp. i9-i9
Author(s):  
Yoshiyuki Fukuda ◽  
Florian Beck ◽  
Wolfgang Baumeister
Keyword(s):  
Electron Tomography ◽  
Molecular Complexes ◽  
Phase Plate ◽  
Structural Studies ◽  
Cryo Electron Tomography ◽  
In Cells

In situ Structure of Viral RNA by Cryo Electron Tomography with Volta Phase Plate, Energy Filtering and Direct Electron Counting

2016 ◽  
Vol 22 (S3) ◽  
pp. 74-75
Author(s):  
Z. Hong Zhou ◽  
Wong H. Hui ◽  
Jiayan Zhang ◽  
Ivo Atanasov ◽  
Cristina C. Celma ◽  
...  
Keyword(s):  
Electron Tomography ◽  
Viral Rna ◽  
Phase Plate ◽  
Energy Filtering ◽  
Electron Counting ◽  
Cryo Electron Tomography

scholarly journals PACRG and FAP20 form the inner junction of axonemal doublet microtubules and regulate ciliary motility

2019 ◽  
Vol 30 (15) ◽  
pp. 1805-1816 ◽  
Author(s):  
Erin E. Dymek ◽  
Jianfeng Lin ◽  
Gang Fu ◽  
Mary E. Porter ◽  
Daniela Nicastro ◽  
...  
Keyword(s):  
Cell Motility ◽  
Electron Tomography ◽  
Structural Studies ◽  
Ciliary Beating ◽  
Ciliary Motility ◽  
Functional Studies ◽  
Cryo Electron Tomography ◽  
Motile Cilia

We previously demonstrated that PACRG plays a role in regulating dynein-driven microtubule sliding in motile cilia. To expand our understanding of the role of PACRG in ciliary assembly and motility, we used a combination of functional and structural studies, including newly identified Chlamydomonas pacrg mutants. Using cryo-electron tomography we show that PACRG and FAP20 form the inner junction between the A- and B-tubule along the length of all nine ciliary doublet microtubules. The lack of PACRG and FAP20 also results in reduced assembly of inner-arm dynein IDA b and the beak-MIP structures. In addition, our functional studies reveal that loss of PACRG and/or FAP20 causes severe cell motility defects and reduced in vitro microtubule sliding velocities. Interestingly, the addition of exogenous PACRG and/or FAP20 protein to isolated mutant axonemes restores microtubule sliding velocities, but not ciliary beating. Taken together, these studies show that PACRG and FAP20 comprise the inner junction bridge that serves as a hub for both directly modulating dynein-driven microtubule sliding, as well as for the assembly of additional ciliary components that play essential roles in generating coordinated ciliary beating.

scholarly journals Actin Organization in Cells Responding to a Perforated Surface, Revealed by Live Imaging and Cryo-Electron Tomography

Structure ◽  
2016 ◽  
Vol 24 (7) ◽  
pp. 1031-1043 ◽  
Author(s):  
Marion Jasnin ◽  
Mary Ecke ◽  
Wolfgang Baumeister ◽  
Günther Gerisch
Keyword(s):  
Electron Tomography ◽  
Live Imaging ◽  
Actin Organization ◽  
Cryo Electron Tomography ◽  
In Cells

scholarly journals Phase Contrast Cryo-Electron Tomography and Single Particle Analysis with a New Phase Plate

2014 ◽  
Vol 20 (S3) ◽  
pp. 232-233
Author(s):  
Maryam Khoshouei ◽  
Radostin Danev ◽  
Günther Gerisch ◽  
Maria Ecke ◽  
Juergen Plitzko ◽  
...  
Keyword(s):  
Single Particle ◽  
Phase Contrast ◽  
Electron Tomography ◽  
Particle Analysis ◽  
Phase Plate ◽  
Single Particle Analysis ◽  
Cryo Electron Tomography ◽  
New Phase

scholarly journals Different functional states of fusion protein gB revealed on human cytomegalovirus by cryo electron tomography with Volta phase plate

2018 ◽  
Vol 14 (12) ◽  
pp. e1007452 ◽  
Author(s):  
Zhu Si ◽  
Jiayan Zhang ◽  
Sakar Shivakoti ◽  
Ivo Atanasov ◽  
Chang-Lu Tao ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Human Cytomegalovirus ◽  
Electron Tomography ◽  
Phase Plate ◽  
Cryo Electron Tomography ◽  
Functional States

scholarly journals Cryo-electron tomography structure of Arp2/3 complex in cells reveals new insights into the branch junction

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Florian Fäßler ◽  
Georgi Dimchev ◽  
Victor-Valentin Hodirnau ◽  
William Wan ◽  
Florian K. M. Schur
Keyword(s):  
Actin Filament ◽  
Electron Tomography ◽  
Active Conformation ◽  
Structural Rearrangements ◽  
Cryo Electron Tomography ◽  
Complex Structural ◽  
Filament Networks ◽  
Subtomogram Averaging ◽  
Resolution Structure ◽  
In Cells

AbstractThe actin-related protein (Arp)2/3 complex nucleates branched actin filament networks pivotal for cell migration, endocytosis and pathogen infection. Its activation is tightly regulated and involves complex structural rearrangements and actin filament binding, which are yet to be understood. Here, we report a 9.0 Å resolution structure of the actin filament Arp2/3 complex branch junction in cells using cryo-electron tomography and subtomogram averaging. This allows us to generate an accurate model of the active Arp2/3 complex in the branch junction and its interaction with actin filaments. Notably, our model reveals a previously undescribed set of interactions of the Arp2/3 complex with the mother filament, significantly different to the previous branch junction model. Our structure also indicates a central role for the ArpC3 subunit in stabilizing the active conformation.

scholarly journals Structural Analysis of Hemagglutinin-Induced Hemifusion by Volta Phase-Plate Cryo-Electron Tomography

2016 ◽  
Vol 110 (3) ◽  
pp. 250a-251a
Author(s):  
Petr Chlanda ◽  
Elena Mekhedov ◽  
Hang Waters ◽  
Cindi L. Schwartz ◽  
Elizabeth R. Fischer ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Electron Tomography ◽  
Phase Plate ◽  
Cryo Electron Tomography

scholarly journals Requirements for Phase-Plate Cryo-Electron Tomography

2010 ◽  
Vol 16 (S2) ◽  
pp. 546-547
Author(s):  
M Marko ◽  
C Hsieh ◽  
A Leith ◽  
C Mannella
Keyword(s):  
Electron Tomography ◽  
Phase Plate ◽  
Cryo Electron Tomography

Extended abstract of a paper presented at Microscopy and Microanalysis 2010 in Portland, Oregon, USA, August 1 – August 5, 2010.

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