Control of protein crystal nucleation around the metastable liquid–liquid phase boundary
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- Oleg Galkin
- Center for Microgravity and Materials Research, and Department of Chemistry, University of Alabama, Huntsville, AL 35899
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- Peter G. Vekilov
- Center for Microgravity and Materials Research, and Department of Chemistry, University of Alabama, Huntsville, AL 35899
書誌事項
- 公開日
- 2000-05-23
- DOI
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- 10.1073/pnas.110000497
- 公開者
- National Academy of Sciences
この論文をさがす
説明
<jats:p>The capability to enhance or suppress the nucleation of protein crystals opens opportunities in various fundamental and applied areas, including protein crystallography, production of protein crystalline pharmaceuticals, protein separation, and treatment of protein condensation diseases. Herein, we show that the rate of homogeneous nucleation of lysozyme crystals passes through a maximum in the vicinity of the liquid–liquid phase boundary hidden below the liquidus (solubility) line in the phase diagram of the protein solution. We found that glycerol and polyethylene glycol (which do not specifically bind to proteins) shift this phase boundary and significantly suppress or enhance the crystal nucleation rates, although no simple correlation exists between the action of polyethylene glycol on the phase diagram and the nucleation kinetics. The control mechanism does not require changes in the protein concentration, acidity, and ionicity of the solution. The effects of the two additives on the phase diagram strongly depend on their concentration, which provides opportunities for further tuning of nucleation rates.</jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 97 (12), 6277-6281, 2000-05-23
National Academy of Sciences
