In vitro analysis of the trajectories of adhesive microbubbles approaching endothelial cells

2020 ◽  
Vol 578 ◽  
pp. 758-767
Author(s):  
Barbara Cerroni ◽  
Flavia Righi Riva ◽  
Letizia Oddo ◽  
Fabio Domenici ◽  
Elisabetta Tortorella ◽  
...  
2015 ◽  
Vol 41 (5) ◽  
pp. 663-670 ◽  
Author(s):  
Waruna Lakmal Dissanayaka ◽  
Lifang Zhu ◽  
Kenneth M. Hargreaves ◽  
Lijian Jin ◽  
Chengfei Zhang

2007 ◽  
Vol 16 (3) ◽  
pp. 141-148 ◽  
Author(s):  
Jörg Borges ◽  
Matthias C. Müller ◽  
Arash Momeni ◽  
G. Björn Stark ◽  
Nestor Torio‐Padron

2020 ◽  
Vol 197 ◽  
pp. 108114
Author(s):  
Diana Amador-Muñoz ◽  
Ángela María Gutiérrez ◽  
César Payán-Gómez ◽  
Luisa Marina Matheus

Author(s):  
R.A. Milligan ◽  
P.N.T. Unwin

A detailed understanding of the mechanism of protein synthesis will ultimately depend on knowledge of the native structure of the ribosome. Towards this end we have investigated the low resolution structure of the eukaryotic ribosome embedded in frozen buffer, making use of a system in which the ribosomes crystallize naturally.The ribosomes in the cells of early chicken embryos form crystalline arrays when the embryos are cooled at 4°C. We have developed methods to isolate the stable unit of these arrays, the ribosome tetramer, and have determined conditions for the growth of two-dimensional crystals in vitro, Analysis of the proteins in the crystals by 2-D gel electrophoresis demonstrates the presence of all ribosomal proteins normally found in polysomes. There are in addition, four proteins which may facilitate crystallization. The crystals are built from two oppositely facing P4 layers and the predominant crystal form, accounting for >80% of the crystals, has the tetragonal space group P4212, X-ray diffraction of crystal pellets demonstrates that crystalline order extends to ~ 60Å.


Sign in / Sign up

Export Citation Format

Share Document