Promoting crystallization of intrinsic membrane proteins with conjugated micelles
Autor: | Kwang-Hwan Jung, Mordechai Sheves, Ellen Wachtel, Noga Friedman, Guy Patchornik, Thien Van Truong, Mihir Ghosh |
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Jazyk: | angličtina |
Rok vydání: | 2020 |
Předmět: |
0301 basic medicine
Thioglucosides Nucleation lcsh:Medicine Crystal growth 02 engineering and technology Micelle Article law.invention Divalent 03 medical and health sciences Nickel law Amphiphile Electron microscopy Ferrous Compounds Crystallization lcsh:Science Micelles X-ray crystallography Chelating Agents chemistry.chemical_classification Multidisciplinary biology Chemistry lcsh:R Bacteriorhodopsin 021001 nanoscience & nanotechnology Zinc Crystallography 030104 developmental biology Ionic strength Bacteriorhodopsins biology.protein lcsh:Q 0210 nano-technology |
Zdroj: | Scientific Reports, Vol 10, Iss 1, Pp 1-9 (2020) Scientific Reports |
ISSN: | 2045-2322 |
Popis: | A new technique for promoting nucleation and growth of membrane protein (MP) crystals from micellar environments is reported. It relies on the conjugation of micelles that sequester MPs in protein detergent complexes (PDCs). Conjugation via amphiphilic [metal:chelator] complexes presumably takes place at the micelle/water interface, thereby bringing the PDCs into proximity, promoting crystal nucleation and growth. We have successfully applied this approach to two light-driven proton pumps: bacteriorhodopsin (bR) and the recently discovered King Sejong 1–2 (KS1–2), using the amphiphilic 4,4′-dinonyl-2,2′-dipyridyl (Dinonyl) (0.7 mM) chelator in combination with Zn2+, Fe2+, or Ni2+ (0.1 mM). Crystal growth in the presence of the [metal–chelator] complexes leads to purple, hexagonal crystals (50–75 µm in size) of bR or pink, rectangular/square crystals (5–15 µm) of KS1–2. The effects of divalent cation identity and concentration, chelator structure and concentration, ionic strength and pH on crystal size, morphology and process kinetics, are described. |
Databáze: | OpenAIRE |
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