page_title: Protein crystallization
section_title: The basics of protein crystallization
hierarchical_section_title: Protein crystallization / The basics of protein crystallization
caption_attribution_description: English: Lysozyme crystals observed through polarizing filter in Nikon SMZ800 microscope. Polarizer is a simple solution to distinguish protein crystals from salt crsytals due to their optical differences, saving time and money measuring salt crystal in diffractometer. Eesti: Lüsosüümi kristallid vaadatuna Nikon SMZ800 mikroskoobist läbi lineaarselt polariseeriva filtri. Polariseeriv filter aitab kristallimise teaduses lihtsa võimaluse eristada valgu kristalli soolakristallist, kuna valgu kristall on valguse suhtes enamikel juhtudel anisotroopne, soolakristallid tihti mitte. Soolakristalli mõõtmine difraktomeetri või sünkrotroniga oleks aga aja ja ressursside kulu. Lüsosüüm on levinud ensüüm (esineb näteks süljes ja munavalges) ning selle eraldamise lihtsus oli üks põhjusi, miks lüsosüüm oli esimene ensüüm, mille struktuur röntgenkiirguse difraktsioonimeetodil lahendati. Võrreldes enamike teiste ensüümide ja valkudega on lüsosüümist lihtne kristalle saada. Antud kristallid on kasvatatud 4 Celsiuse kraadi juures NaCl tingimustes "batch" (partii) meetodil. Pilt on tehtud nutitelefoniga Samsung Galaxy SII (kaamerasilma suurus on sobilik mikroskoobi okulaari avaga) Tromsø Ülikooli Norstruct laboris.
context_page_description: 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.
  In the process of protein crystallization, proteins are dissolved in an aqueous environment and sample solution until they reach the supersaturated state. 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. 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.
caption: Lysozyme crystals observed through polarizing filter.
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