Gel Formation of Oxidized Cellulose and Improving Protein Purification

Aqueous solutions of tryptophan synthase (TS) must be prepared with sufficient homogeneity to promote growth of crystals. Such crystals must be large and defect-free to allow effective analysis with neutron diffraction (ND). Aggregates, which disrupt crystal growth, must be removed through precipitation and dissolution. Two precipitation methods were analyzed using dynamic light scattering (DLS). The first method was a single-step addition of precipitant and the second was a three-step addition over a period of 48 hours. DLS revealed that the second precipitation procedure yielded the TS solution with the lowest aggregate content. Slow precipitation therefore produces TS solutions that are most favorable for growth of crystals suitable for ND.
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Abstract/Description: Aqueous solutions of tryptophan synthase (TS) must be prepared with sufficient homogeneity to promote growth of crystals. Such crystals must be large and defect-free to allow effective analysis with neutron diffraction (ND). Aggregates, which disrupt crystal growth, must be removed through precipitation and dissolution. Two precipitation methods were analyzed using dynamic light scattering (DLS). The first method was a single-step addition of precipitant and the second was a three-step addition over a period of 48 hours. DLS revealed that the second precipitation procedure yielded the TS solution with the lowest aggregate content. Slow precipitation therefore produces TS solutions that are most favorable for growth of crystals suitable for ND.
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