4.8 Article

Growth Rates of Protein Crystals

Journal

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 134, Issue 9, Pages 3934-3937

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/ja207336r

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Funding

  1. NIH [GM34993]

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Protein crystallization is important for structural biology. The rate at which a protein crystallizes is often the bottleneck in determining the protein's structure. Here, we give a physical model for the growth rates of protein crystals. Most materials crystallize faster under stronger growth conditions; however, protein crystallization slows down under the strongest conditions. Proteins require a crystallization slot of 'just right' conditions. Our model provides an explanation. Unlike simpler materials, proteins are orientationally asymmetrical. Under strong conditions, protein molecules attempt to crystallize too quickly, in wrong orientations, blocking surface sites for more productive crystal growth. The model explains the observation that increasing the net charge on a protein increases the crystal growth rate. The model predictions are in good agreement with experiments on the growth rates of tetragonal lysozyme crystals as a function of pH, salt concentration, temperature, and protein concentration.

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