This article focuses too much on specific examples. Please help improve this article by adding sources that evaluate within a broader context.(December 2013)
Crystals of proteins grown on the U.S. Space Shuttle or Russian Space Station, Mir.
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]
In the process of protein crystallization, proteins are dissolved in an aqueous environment and sample solution until they reach the supersaturated state.[3] Different methods are used to reach that state such as vapor diffusion, microbatch, microdialysis, and free-interface diffusion. 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][5]
^Schey KL, Wang Z, L Wenke J, Qi Y (May 2014). "Aquaporins in the eye: expression, function, and roles in ocular disease". Biochimica et Biophysica Acta (BBA) - General Subjects. 1840 (5): 1513–1523. doi:10.1016/j.bbagen.2013.10.037. PMC 4572841. PMID 24184915.
^Gonen T, Cheng Y, Sliz P, Hiroaki Y, Fujiyoshi Y, Harrison SC, Walz T (December 2005). "Lipid-protein interactions in double-layered two-dimensional AQP0 crystals". Nature. 438 (7068): 633–638. Bibcode:2005Natur.438..633G. doi:10.1038/nature04321. PMC 1350984. PMID 16319884.
^ abMcPherson A, Gavira JA (January 2014). "Introduction to protein crystallization". Acta Crystallographica. Section F, Structural Biology Communications. 70 (Pt 1): 2–20. doi:10.1107/s2053230x13033141. PMC 3943105. PMID 24419610.
^Blundell TL (July 2017). "Protein crystallography and drug discovery: recollections of knowledge exchange between academia and industry". IUCrJ. 4 (Pt 4): 308–321. doi:10.1107/s2052252517009241. PMC 5571795. PMID 28875019.
^Tripathy D, Bardia A, Sellers WR (July 2017). "Ribociclib (LEE011): Mechanism of Action and Clinical Impact of This Selective Cyclin-Dependent Kinase 4/6 Inhibitor in Various Solid Tumors". Clinical Cancer Research. 23 (13): 3251–3262. doi:10.1158/1078-0432.ccr-16-3157. PMC 5727901. PMID 28351928.
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