Crystallization (disambiguation)

Last updated

Crystallization is the (natural or artificial) formation of highly organized, solid crystals.

Crystallization or Crystallize may also refer to:

Related Research Articles

X-ray crystallography Technique used in studying crystal structure

X-ray crystallography (XRC) is the experimental science determining the atomic and molecular structure of a crystal, in which the crystalline structure causes a beam of incident X-rays to diffract into many specific directions. By measuring the angles and intensities of these diffracted beams, a crystallographer can produce a three-dimensional picture of the density of electrons within the crystal. From this electron density, the mean positions of the atoms in the crystal can be determined, as well as their chemical bonds, their crystallographic disorder, and various other information.

Marshmallow Sugar-based confection

Marshmallow is a type of confectionery that is typically made from sugar, water and gelatin whipped to a squishy consistency. It is used as a filling in baking, or commonly molded into shapes and coated with corn starch. This is the modern version of a medicinal confection made from Althaea officinalis, the marshmallow plant.

Differential scanning calorimetry

Differential scanning calorimetry (DSC) is a thermoanalytical technique in which the difference in the amount of heat required to increase the temperature of a sample and reference is measured as a function of temperature. Both the sample and reference are maintained at nearly the same temperature throughout the experiment. Generally, the temperature program for a DSC analysis is designed such that the sample holder temperature increases linearly as a function of time. The reference sample should have a well-defined heat capacity over the range of temperatures to be scanned.

Integral membrane protein

An integral membrane protein (IMP) is a type of membrane protein that is permanently attached to the biological membrane. All transmembrane proteins are IMPs, but not all IMPs are transmembrane proteins. IMPs comprise a significant fraction of the proteins encoded in an organism's genome. Proteins that cross the membrane are surrounded by annular lipids, which are defined as lipids that are in direct contact with a membrane protein. Such proteins can only be separated from the membranes by using detergents, nonpolar solvents, or sometimes denaturing agents.

Structural genomics

Structural genomics seeks to describe the 3-dimensional structure of every protein encoded by a given genome. This genome-based approach allows for a high-throughput method of structure determination by a combination of experimental and modeling approaches. The principal difference between structural genomics and traditional structural prediction is that structural genomics attempts to determine the structure of every protein encoded by the genome, rather than focusing on one particular protein. With full-genome sequences available, structure prediction can be done more quickly through a combination of experimental and modeling approaches, especially because the availability of large number of sequenced genomes and previously solved protein structures allows scientists to model protein structure on the structures of previously solved homologs.

Thaumatin

Thaumatin is a low-calorie sweetener and flavour modifier. The protein is often used primarily for its flavour-modifying properties and not exclusively as a sweetener.

John Howard Northrop

John Howard Northrop was an American biochemist who, with James Batcheller Sumner and Wendell Meredith Stanley, won the 1946 Nobel Prize in Chemistry. The award was given for these scientists' isolation, crystallization, and study of enzymes, proteins, and viruses. Northrop was a Professor of Bacteriology and Medical Physics, Emeritus, at University of California, Berkeley.

James B. Sumner

James Batcheller Sumner was an American chemist. He discovered that enzymes can be crystallized, for which he shared the Nobel Prize in Chemistry in 1946 with John Howard Northrop and Wendell Meredith Stanley. He was also the first to prove that enzymes are proteins.

Fractionation

Fractionation is a separation process in which a certain quantity of a mixture is divided during a phase transition, into a number of smaller quantities (fractions) in which the composition varies according to a gradient. Fractions are collected based on differences in a specific property of the individual components. A common trait in fractionations is the need to find an optimum between the amount of fractions collected and the desired purity in each fraction. Fractionation makes it possible to isolate more than two components in a mixture in a single run. This property sets it apart from other separation techniques.

Salting out is an effect based on the electrolyte–non-electrolyte interaction, in which the non-electrolyte could be less soluble at high salt concentrations. It is used as a method of purification for proteins, as well as preventing protein denaturation due to excessively diluted samples during experiments. The salt concentration needed for the protein to precipitate out of the solution differs from protein to protein. This process is also used to concentrate dilute solutions of proteins. Dialysis can be used to remove the salt if needed.

Crystallization

Crystallization or crystallisation is the process by which a solid forms, where the atoms or molecules are highly organized into a structure known as a crystal. Some of the ways by which crystals form are precipitating from a solution, freezing, or more rarely deposition directly from a gas. Attributes of the resulting crystal depend largely on factors such as temperature, air pressure, and in the case of liquid crystals, time of fluid evaporation.

A crystallization adjutant is a material used to promote crystallization, normally in a context where a material does not crystallize naturally from a pure solution.

Sorbitol dehydrogenase is a cytosolic enzyme. In humans this protein is encoded by the SORD gene.

<i>beta</i>-Amanitin Cyclic peptide part of a group of toxins present in Amanita mushrooms

beta-Amanitin or β-amanitin is a cyclic peptide comprising eight amino acids. It is part of a group of toxins called amatoxins, which can be found in several mushrooms belonging to the genus Amanita. Some examples are the death cap and members of the destroying angel complex, which includes A. virosa and A. bisporigera. Due to the presence of α-amanitin, β-amanitin, γ-amanitin and ε-amanitin these mushrooms are highly lethal to human beings.

Tau-protein kinase Class of enzymes

In enzymology, a tau-protein kinase is an enzyme that catalyzes the chemical reaction

Scientific research on the International Space Station

Scientific research on the International Space Station is a collection of experiments that require one or more of the unusual conditions present in low Earth orbit. The primary fields of research include human research, space medicine, life sciences, physical sciences, astronomy and meteorology. The 2005 NASA Authorization Act designated the American segment of the International Space Station as a national laboratory with the goal of increasing the use of the ISS by other federal agencies and the private sector.

Protein crystallization process of formation of a protein crystal

Protein crystallization is the process of formation of a regular array of individual protein molecules stabilized by crystal contacts. If the crystal is sufficiently ordered, it will diffract. Some proteins naturally form crystalline arrays, like aquaporin in the lens of the eye.

Crystallize (Kylie Minogue song) 2014 song by Kylie Minogue

"Crystallize" is a song by Australian recording artist Kylie Minogue. It was written by Minogue, Dev Hynes and Scott Hoffman. The song was originally recorded for Minogue's 2014 album, Kiss Me Once, but did not make the final cut.

Moses Kunitz (1887–1978) was a Russian-American biochemist who spent most of his career at Rockefeller University. He is best known for a series of experiments in purification and crystallization of proteins, contributing to the determination that enzymes are proteins.

Naomi Chayen is a biochemist and structural biologist. She is a professor of Biomedical Sciences at Imperial College London, where she leads the Crystallization Group in Computational and Systems Medicine. She is best known for developing the microbatch method and inventing novel nucleants for protein crystallization which have been applied to high-throughput screening for rational drug design.