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Crystal habits of the protein thaumatin crystallized with sodium DL-tartrate at 4 °C and

Precipitant Chirality and Protein Crystallization Neer R. Asherie , Yeshiva University, DMR 0901260.

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Crystal habits of the protein thaumatin crystallized with sodium DL-tartrate at 4 °C and

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  1. Precipitant Chirality and Protein CrystallizationNeerR. Asherie, Yeshiva University, DMR 0901260 Protein self-assembly is not well understood. For example, we are unable to predict what will happen to a homogeneous solution of a protein when the conditions are changed. Our long-term goal is to make it possible to predict the phase behavior of protein solutions and to learn to control protein self-assembly. We are currently focusing on recent discovery made in our laboratory: the stereoisomerism of precipitants can radically alter the crystallization of globular proteins. For example, the chirality of the precipitant can affect the crystal habit, crystal solubility and the kinetics of nucleation and growth. Crystal habits of the protein thaumatin crystallized with sodium DL-tartrate at 4 °C and 19 °C. Scale bar is 100 microns. A B

  2. Undergraduate involvement in research on protein self-assembly NeerR. Asherie, Yeshiva University, DMR 0901260 Undergraduates are an essential part of research at an RUI institution. The Asherie research group consists of several undergraduates who work together with the PI in the lab. Samuel Blass (left), an undergraduate researcher in the Asherie lab for three years, received an NSF Graduate Fellowship and is studying Materials Science at the University of Minnesota. The most recent publication from the lab features several undergraduate co-authors (denoted with an asterisk): N. Asherie, J. Jakoncic, C. Ginsberg*, A. Greenbaum*, V. Stojanoff, B. Hrnjez, S. Blass* and J. Berger*, “Tartrate chirality determines thaumatin crystal habit,” Cryst. Growth Des.9, 4189-4198 (2009). 

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