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Crystallization is the process by which solids form, where the atoms or molecules are highly organized into a structure known as a crystal.Some ways by which crystals form are precipitating from a solution, freezing, or more rarely deposition directly from a gas.
Biocrystallization is the formation of crystals from organic macromolecules by living organisms. [1] This may be a stress response, a normal part of metabolism such as processes that dispose of waste compounds, or a pathology. Template mediated crystallization is qualitatively different from in vitro crystallization.
Consider the average number of particles with particle properties denoted by a particle state vector (x,r) (where x corresponds to particle properties like size, density, etc. also known as internal coordinates and, r corresponds to spatial position or external coordinates) dispersed in a continuous phase defined by a phase vector Y(r,t) (which again is a function of all such vectors which ...
The equation was first derived by Johnson, Mehl, Avrami and Kolmogorov (in Russian) in a series of articles published in the Journal of Chemical Physics between 1939 and 1941. [2] [3] [4] Moreover, Kolmogorov treated statistically the crystallization of a solid in 1937 (in Russian, Kolmogorov, A. N., Izv. Akad. Nauk. SSSR., 1937, 3, 355).
Crystallization affects optical, mechanical, thermal and chemical properties of the polymer. The degree of crystallinity is estimated by different analytical methods and it typically ranges between 10 and 80%, with crystallized polymers often called "semi-crystalline". The properties of semi-crystalline polymers are determined not only by the ...
Proteins generally absorb light at 280 nanometers due to the presence of tryptophan and tyrosine. Nucleic acids absorb more at 260 nm, primarily due to purine and pyrimidine bases. The Warburg–Christian method combines measurements at these wavelengths to estimate the amounts of protein and nucleic acid present. [ 1 ]
Salting out (also known as salt-induced precipitation, salt fractionation, anti-solvent crystallization, precipitation crystallization, or drowning out) [1] is a purification technique that utilizes the reduced solubility of certain molecules in a solution of very high ionic strength.
Developing protein crystals is a difficult process influenced by many factors, including pH, temperature, ionic strength in the crystallization solution, and even gravity. [3] Once formed, these crystals can be used in structural biology to study the molecular structure of the protein, particularly for various industrial or medical purposes.