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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. [1] [2]
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 .
Racemic crystal structure of Rv1738 from Mycobacterium tuberculosis produced by racemic protein crystallography. Racemic crystallography is a technique used in structural biology where crystals of a protein molecule are developed from an equimolar mixture of an L-protein molecule of natural chirality and its D-protein mirror image.
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.
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]
The endocrine system is a complex network of glands and organs that produce and release hormones which control many of our body’s basic functions, such as metabolism, growth and reproduction.
A crystal system is a set of point groups in which the point groups themselves and their corresponding space groups are assigned to a lattice system. Of the 32 point groups that exist in three dimensions, most are assigned to only one lattice system, in which case the crystal system and lattice system both have the same name.
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