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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.
Nitrocellulose slides are used mainly in proteomics to do protein microarrays with automated systems that print the slides and record results. Microarrays of cell analytes, arrays of cell lysate, antibody microarrays, tissue printing, [1] [2] immunoarrays, etc. are also possible with the slide.
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.
Protein crystals are scooped up by a loop, then flash-frozen with liquid nitrogen. [108] This freezing reduces the radiation damage of the X-rays, as well as thermal motion (the Debye-Waller effect). However, untreated protein crystals often crack if flash-frozen; therefore, they are generally pre-soaked in a cryoprotectant solution before ...
Streak seeding [1] is a method first described during ICCBM-3 by Enrico Stura to induce crystallization in a straight line into a sitting or hanging drop for protein crystallization by introducing microseeds. The purpose is to control nucleation and understand the parameters that make crystals grow. It is also used to test any particular set of ...
Ammonium sulfate is an inorganic salt with a high solubility that disassociates into ammonium (NH + 4) and sulfate (SO 2− 4) in aqueous solutions. [1] Ammonium sulfate is especially useful as a precipitant because it is highly soluble, stabilizes protein structure, has a relatively low density, is readily available, and is relatively inexpensive.
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.
Protein crystallization is more successful for proteins with a higher melting point [8] and adding buffer components that stabilize proteins improve the likelihood of protein crystals forming. [9] If examining pH then the possible effects of the buffer molecule on thermal stability should be taken into account along with the fact that pKa of ...