Analyzing the Variability of the 3D Structure of Chromatin Fiber Using Statistical Shape Theory

Author(s):  
Siwei Yang ◽  
Sandra Götze ◽  
Julio Mateos-Langerak ◽  
Roel van Driel ◽  
Roland Eils ◽  
...  
2013 ◽  
Vol 114 ◽  
pp. 29-39
Author(s):  
Francisco J. Caro-Lopera ◽  
Graciela González-Farías ◽  
N. Balakrishnan

2008 ◽  
Vol 1783 (11) ◽  
pp. 2089-2099 ◽  
Author(s):  
Siwei Yang ◽  
Doris Illner ◽  
Kathrin Teller ◽  
Irina Solovei ◽  
Roel van Driel ◽  
...  

2010 ◽  
pp. 131-147
Author(s):  
Siwei Yang ◽  
Doris Illner ◽  
Kathrin Teller ◽  
Irina Solovei ◽  
Roel van Driel ◽  
...  

Author(s):  
Wilfrid S. Kendall ◽  
Huiling Le

2014 ◽  
Vol 31 (2) ◽  
pp. 160-177 ◽  
Author(s):  
Javier Cano ◽  
Javier M. Moguerza ◽  
Stelios Psarakis ◽  
Athanasios N. Yannacopoulos

Author(s):  
A. Engel ◽  
D.L. Dorset ◽  
A. Massalski ◽  
J.P. Rosenbusch

Porins represent a group of channel forming proteins that facilitate diffusion of small solutes across the outer membrane of Gram-negative bacteria, while excluding large molecules (>650 Da). Planar membranes reconstituted from purified matrix porin (OmpF protein) trimers and phospholipids have allowed quantitative functional studies of the voltage-dependent channels and revealed concerted activation of triplets. Under the same reconstitution conditions but using high protein concentrations porin aggregated to 2D lattices suitable for electron microscopy and image processing. Depending on the lipid-to- protein ratio three different crystal packing arrangements were observed: a large (a = 93 Å) and a small (a = 79 Å) hexagonal and a rectangular (a = 79 Å b = 139 Å) form with p3 symmetry for the hexagonal arrays. In all crystal forms distinct stain filled triplet indentations could be seen and were found to be morphologically identical within a resolution of (22 Å). It is tempting to correlate stain triplets with triple channels, but the proof of this hypothesis requires an analysis of the structure in 3 dimensions.


Author(s):  
Vijay Krishnamurthi ◽  
Brent Bailey ◽  
Frederick Lanni

Excitation field synthesis (EFS) refers to the use of an interference optical system in a direct-imaging microscope to improve 3D resolution by axially-selective excitation of fluorescence within a specimen. The excitation field can be thought of as a weighting factor for the point-spread function (PSF) of the microscope, so that the optical transfer function (OTF) gets expanded by convolution with the Fourier transform of the field intensity. The simplest EFS system is the standing-wave fluorescence microscope, in which an axially-periodic excitation field is set up through the specimen by interference of a pair of collimated, coherent, s-polarized beams that enter the specimen from opposite sides at matching angles. In this case, spatial information about the object is recovered in the central OTF passband, plus two symmetric, axially-shifted sidebands. Gaps between these bands represent "lost" information about the 3D structure of the object. Because the sideband shift is equal to the spatial frequency of the standing-wave (SW) field, more complete recovery of information is possible by superposition of fields having different periods. When all of the fields have an antinode at a common plane (set to be coincident with the in-focus plane), the "synthesized" field is peaked in a narrow infocus zone.


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