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| Hauptseite > Publikationsdatenbank > Expression and purification of arrestin in yeast Saccharomyces cerevisiae |
| Hauptseite > Publikationsdatenbank > Expression and purification of arrestin in yeast Saccharomyces cerevisiae |
| Contribution to a book | FZJ-2017-07056 |
; ; ;
2017
Academic Press
San Diego, US
Abstract: Protein purity and yield are two critical parameters for successful protein characterization using structural techniques such as X-ray crystallography, NMR, and several other biophysical methods. The yeast Saccharomyces cerevisiae is one of the popular eukaryotic model systems for overexpression and subsequent purification of recombinant proteins. Here, we describe a protocol for cloning, overexpression, purification, and crystallization of arrestin-1 and its splice variant p44 from yeast. The purification protocol involves a single-affinity chromatography step on a Strep-Tactin column. Highly purified arrestins can be concentrated up to 15 mg/mL using ultrafiltration and can be stored in the frozen state for several months without any loss of functionality.
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