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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. [4 ...
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.
A cholesterol crystal is a solid, crystalline form of cholesterol found in gallstones and atherosclerosis. Gallstones occurring in industrialized societies typically contain more than 70-90% cholesterol by weight, much of which is crystalline. [ 1 ]
Parts-per-million cube of relative abundance by mass of elements in an average adult human body down to 1 ppm. About 99% of the mass of the human body is made up of six elements: oxygen, carbon, hydrogen, nitrogen, calcium, and phosphorus. Only about 0.85% is composed of another five elements: potassium, sulfur, sodium, chlorine, and magnesium ...
[1] [2] The body then traps the released iron and stores it as hemosiderin in tissues. [3] Hemosiderin is also generated from the abnormal metabolic pathway of ferritin. [3] It is only found within cells (as opposed to circulating in blood) and appears to be a complex of ferritin, denatured ferritin and other material.
Crystallopathy is a harmful state or disease associated with the formation and aggregation of crystals in tissues or cavities, [1] [2] or in other words, a heterogeneous group of diseases caused by intrinsic or environmental microparticles or crystals, promoting tissue inflammation and scarring.
In addition, physical properties are often controlled by crystalline defects. The understanding of crystal structures is an important prerequisite for understanding crystallographic defects. Most materials do not occur as a single crystal, but are poly-crystalline in nature (they exist as an aggregate of small crystals with different orientations).
1997 - The X-ray crystal structure of bacteriorhodopsin was the first time the lipidic cubic phase (LCP) was used to facilitate the crystallization of a membrane protein; LCP has since been used to obtain the structures of many unique membrane proteins, including G protein-coupled receptors (GPCRs). [235]