Is Stereoscopic Capture Possible with Three-Dimensionally Slanted or Curved Illusory Surfaces?

Perception ◽  
1996 ◽  
Vol 25 (1_suppl) ◽  
pp. 73-73
Author(s):  
J Häkkinen ◽  
M Liinasuo ◽  
I Kojo ◽  
G Nyman

The depth of disparate illusory contours affects the perception of background patterns that are enclosed by these contours. If the pattern is repetitive, the depth of the illusory surface is attributed to texture elements even though the texture is in zero disparity. Previous results have suggested that this phenomenon, called stereoscopic capture, is possible only with frontoparallel surfaces (Ramachandran, 1986 Perception & Psychophysics39 361 – 373). We hypothesised that the disruption of stereo capture with three-dimensionally slanted or curved surfaces has been due to the impossibility of consistent rematching of background texture elements. If the texture is designed in such a way that adjacent elements can be rematched to form a surface that is consistent with the three-dimensional structure of the illusory surface, the capture should be possible with complex surfaces. We investigated our hypothesis by showing three-dimensionally slanted and curved surfaces to subjects and changing the pattern of the background texture. According to our results a texture of a constant period can be captured only by a frontoparallel surface; however, if the texture is designed to be consistent with the three-dimensional structure of the complex surface, the texture elements that initially form a frontoparallel surface form a complex surface when they are captured. We conclude that (a) stereoscopic capture is possible with complex three-dimensional surfaces; (b) the possible discrete matches within the background texture determine the possible three-dimensional forms that can be captured and therefore stereoscopic capture should not be characterised only as depth interpolation (Mitchison and McKee, 1987 Vision Research27 285 – 294) between large image elements.

Author(s):  
N. H. Olson ◽  
T. S. Baker ◽  
Wu Bo Mu ◽  
J. E. Johnson ◽  
D. A. Hendry

Nudaurelia capensis β virus (NβV) is an RNA virus of the South African Pine Emperor moth, Nudaurelia cytherea capensis (Lepidoptera: Saturniidae). The NβV capsid is a T = 4 icosahedron that contains 60T = 240 subunits of the coat protein (Mr = 61,000). A three-dimensional reconstruction of the NβV capsid was previously computed from visions embedded in negative stain suspended over holes in a carbon film. We have re-examined the three-dimensional structure of NβV, using cryo-microscopy to examine the native, unstained structure of the virion and to provide a initial phasing model for high-resolution x-ray crystallographic studiesNβV was purified and prepared for cryo-microscopy as described. Micrographs were recorded ∼1 - 2 μm underfocus at a magnification of 49,000X with a total electron dose of about 1800 e-/nm2.


Author(s):  
David A. Agard ◽  
Yasushi Hiraoka ◽  
John W. Sedat

In an effort to understand the complex relationship between structure and biological function within the nucleus, we have embarked on a program to examine the three-dimensional structure and organization of Drosophila melanogaster embryonic chromosomes. Our overall goal is to determine how DNA and proteins are organized into complex and highly dynamic structures (chromosomes) and how these chromosomes are arranged in three dimensional space within the cell nucleus. Futher, we hope to be able to correlate structual data with such fundamental biological properties as stage in the mitotic cell cycle, developmental state and transcription at specific gene loci.Towards this end, we have been developing methodologies for the three-dimensional analysis of non-crystalline biological specimens using optical and electron microscopy. We feel that the combination of these two complementary techniques allows an unprecedented look at the structural organization of cellular components ranging in size from 100A to 100 microns.


Author(s):  
José L. Carrascosa ◽  
José M. Valpuesta ◽  
Hisao Fujisawa

The head to tail connector of bacteriophages plays a fundamental role in the assembly of viral heads and DNA packaging. In spite of the absence of sequence homology, the structure of connectors from different viruses (T4, Ø29, T3, P22, etc) share common morphological features, that are most clearly revealed in their three-dimensional structure. We have studied the three-dimensional reconstruction of the connector protein from phage T3 (gp 8) from tilted view of two dimensional crystals obtained from this protein after cloning and purification.DNA sequences including gene 8 from phage T3 were cloned, into Bam Hl-Eco Rl sites down stream of lambda promotor PL, in the expression vector pNT45 under the control of cI857. E R204 (pNT89) cells were incubated at 42°C for 2h, harvested and resuspended in 20 mM Tris HC1 (pH 7.4), 7mM 2 mercaptoethanol, ImM EDTA. The cells were lysed by freezing and thawing in the presence of lysozyme (lmg/ml) and ligthly sonicated. The low speed supernatant was precipitated by ammonium sulfate (60% saturated) and dissolved in the original buffer to be subjected to gel nitration through Sepharose 6B, followed by phosphocellulose colum (Pll) and DEAE cellulose colum (DE52). Purified gp8 appeared at 0.3M NaCl and formed crystals when its concentration increased above 1.5 mg/ml.


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