scholarly journals Comparing an Atomic Model or Structure to a Corresponding Cryo-electron Microscopy Image at the Central Axis of a Helix

2017 ◽  
Vol 24 (1) ◽  
pp. 52-67 ◽  
Author(s):  
Stephanie Zeil ◽  
Julio Kovacs ◽  
Willy Wriggers ◽  
Jing He
2017 ◽  
Vol 200 (1) ◽  
pp. 20-27 ◽  
Author(s):  
Jesús Cuenca-Alba ◽  
Laura del Cano ◽  
Josué Gómez Blanco ◽  
José Miguel de la Rosa Trevín ◽  
Pablo Conesa Mingo ◽  
...  

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Julian Hennies ◽  
José Miguel Serra Lleti ◽  
Nicole L. Schieber ◽  
Rachel M. Templin ◽  
Anna M. Steyer ◽  
...  

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Stephen M Hinshaw ◽  
Andrew N Dates ◽  
Stephen C Harrison

Kinetochores are the chromosomal attachment points for spindle microtubules. They are also signaling hubs that control major cell cycle transitions and coordinate chromosome folding. Most well-studied eukaryotes rely on a conserved set of factors, which are divided among two loosely-defined groups, for these functions. Outer kinetochore proteins contact microtubules or regulate this contact directly. Inner kinetochore proteins designate the kinetochore assembly site by recognizing a specialized nucleosome containing the H3 variant Cse4/CENP-A. We previously determined the structure, resolved by cryo-electron microscopy (cryo-EM), of the yeast Ctf19 complex (Ctf19c, homologous to the vertebrate CCAN), providing a high-resolution view of inner kinetochore architecture (Hinshaw and Harrison, 2019). We now extend these observations by reporting a near-atomic model of the Ctf3 complex, the outermost Ctf19c sub-assembly seen in our original cryo-EM density. The model is sufficiently well-determined by the new data to enable molecular interpretation of Ctf3 recruitment and function.


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