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== Protein crystallization == |
== Protein crystallization == |
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'''Protein crystallization''' is the process of formation of a '''protein crystal'''. In the process, proteins will dissolve in an aqueous environment, and be recrystallized by different methods. Such as, '''Vapor diffusion, Microbatch, Microdialysis, Free-interface diffusion,''' etc. Some parameters including pH, temperature, ionic strength in the crystallization solution and other factors will influence the result. |
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Based on the crystal, the determination of protein structure can be achieved traditionally by utilizing X-Ray Diffraction (XRD). Alternatively, cryo-electron microscopy (cryo-EM) and nuclear magnetic resonance (NMR) could also be used for protein structure determination. The structural chemistry of biological macromolecules, such as proteins, is significant due to the need of structural analysis in biochemistry and translational medicine. |
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== Development of protein crystallization == |
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In 1840, Friedrich Ludwig Hünefeld accidentally discovered the formation of crystalline material in samples of the earthworm blood held under two glass slides and occasionally observed small plate‐like crystals in desiccated swine or human blood samples (111111) These crystals ware named as ‘haemoglobin’, by Felix Hoppe‐Seyler in 1864. (22222). |
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Revision as of 14:10, 19 February 2019
 | This is a user sandbox of Dixiang Yuan. You can use it for testing or practicing edits. This is not the sandbox where you should draft your assigned article for a dashboard.wikiedu.org course. To find the right sandbox for your assignment, visit your Dashboard course page and follow the Sandbox Draft link for your assigned article in the My Articles section. |
Protein crystallization
Protein crystallization is the process of formation of a protein crystal. In the process, proteins will dissolve in an aqueous environment, and be recrystallized by different methods. Such as, Vapor diffusion, Microbatch, Microdialysis, Free-interface diffusion, etc. Some parameters including pH, temperature, ionic strength in the crystallization solution and other factors will influence the result.
Based on the crystal, the determination of protein structure can be achieved traditionally by utilizing X-Ray Diffraction (XRD). Alternatively, cryo-electron microscopy (cryo-EM) and nuclear magnetic resonance (NMR) could also be used for protein structure determination. The structural chemistry of biological macromolecules, such as proteins, is significant due to the need of structural analysis in biochemistry and translational medicine.
Development of protein crystallization
In 1840, Friedrich Ludwig Hünefeld accidentally discovered the formation of crystalline material in samples of the earthworm blood held under two glass slides and occasionally observed small plate‐like crystals in desiccated swine or human blood samples (111111) These crystals ware named as ‘haemoglobin’, by Felix Hoppe‐Seyler in 1864. (22222).