Crystallogenesis of bioliquid in the homoeopathy

The term ÃƒÂ¢Ã¢â€šÂ¬Ã…â€œcrystallogenesisÃƒÂ¢Ã¢â€šÂ¬Ã‚Â was primarily mentioned in 1730. I. Newton in his research ÃƒÂ¢Ã¢â€šÂ¬Ã…â€œOpticsÃƒÂ¢Ã¢â€šÂ¬Ã‚Âdescribed a phenomenon of regular structure formation from salt solutions. The latter proved to be the origin of nowadays biocrystallography. Later crystallography has been also applied in pharmacy (medication synthesis) and forensic medicine (toxicology). Moreover, a number of clinically oriented works on crystallography have been issued. This method is simple and safe for investigated people and animals. The purpose of this new medico-biological science is to discover crystallogenesis mechanisms and further to work out the criteria for estimation of various substrates bioinformation and biocrystallisation management on the basis of up-to-date accomplishments in the homoeopathy.

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3D numerical simulation of regular structure formation in a locally heated falling film

European Journal of Mechanics - B/Fluids ◽

10.1016/s0997-7546(03)00056-6 ◽

2003 ◽

Vol 22 (5) ◽

pp. 445-471 ◽

Cited By ~ 31

Author(s):

Alexander M. Frank

Keyword(s):

Numerical Simulation ◽

Structure Formation ◽

Regular Structure ◽

Falling Film ◽

3D Numerical Simulation

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Isomorphous replacement in electron diffraction of wet crystals of rat hemoglobin

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100075968 ◽

1983 ◽

Vol 41 ◽

pp. 446-447

Author(s):

William F. Tivol ◽

Murray Vernon King ◽

D. F. Parsons

Keyword(s):

Electron Diffraction ◽

Heavy Atom ◽

Isomorphous Substitution ◽

X Ray Diffraction ◽

Salt Solutions ◽

X Ray ◽

Isomorphous Replacement ◽

Structure Factors ◽

Diffraction Structure ◽

The Mean

Feasibility of isomorphous substitution in electron diffraction is supported by a calculation of the mean alteration of the electron-diffraction structure factors for hemoglobin crystals caused by substituting two mercury atoms per molecule, following Green, Ingram & Perutz, but with allowance for the proportionality of f to Z3/4 for electron diffraction. This yields a mean net change in F of 12.5%, as contrasted with 22.8% for x-ray diffraction.Use of the hydration chamber in electron diffraction opens prospects for examining many proteins that yield only very thin crystals not suitable for x-ray diffraction. Examination in the wet state avoids treatments that could cause translocation of the heavy-atom labels or distortion of the crystal. Combined with low-fluence techniques, it enables study of the protein in a state as close to native as possible.We have undertaken a study of crystals of rat hemoglobin by electron diffraction in the wet state. Rat hemoglobin offers a certain advantage for hydration-chamber work over other hemoglobins in that it can be crystallized from distilled water instead of salt solutions.

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Bulk standards for low-temperature biological x-ray microanalysis

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100111525 ◽

1984 ◽

Vol 42 ◽

pp. 282-283

Author(s):

P. Echlin ◽

M. McKoon ◽

E.S. Taylor ◽

C.E. Thomas ◽

K.L. Maloney ◽

...

Keyword(s):

Phase Separation ◽

Low Temperature ◽

Analytical Method ◽

Salt Solutions ◽

Absolute Concentration ◽

Cooling Process ◽

X Ray ◽

The Absolute ◽

Analytical Procedures ◽

Electrical Conductors

Although sections of frozen salt solutions have been used as standards for x-ray microanalysis, such solutions are less useful when analysed in the bulk form. They are poor thermal and electrical conductors and severe phase separation occurs during the cooling process. Following a suggestion by Whitecross et al we have made up a series of salt solutions containing a small amount of graphite to improve the sample conductivity. In addition, we have incorporated a polymer to ensure the formation of microcrystalline ice and a consequent homogenity of salt dispersion within the frozen matrix. The mixtures have been used to standardize the analytical procedures applied to frozen hydrated bulk specimens based on the peak/background analytical method and to measure the absolute concentration of elements in developing roots.

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Interrelationship of the cellular distribution and secretion of regular structure (RS) protein in Bacillus licheniformis nm 105

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100123969 ◽

1992 ◽

Vol 50 (1) ◽

pp. 712-713

Author(s):

Xiaorong Zhu ◽

Richard McVeigh ◽

Bijan K. Ghosh

Keyword(s):

Alkaline Phosphatase ◽

Bacillus Licheniformis ◽

Self Assembly ◽

Gel Electrophoresis ◽

Culture Supernatant ◽

Regular Structure ◽

The Self ◽

Cellular Distribution ◽

Structural Protein ◽

Laboratory Cultures

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.

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