Affiliation:
1. University of Chemical Technology and Metallurgy
Abstract
Abstract
Protein molecules, although big and complicated structures, arrange into ordered crystal formations, but at specific only conditions, related to pH, additives and temperature. Truly, their crystallization is still more art than science and conditions relating their behavior to the known rules of crystal growth and dissolution are under investigation. This study is devoted to dissolution and more precise - the influence of undersaturation on the habitus of the dissolving tetragonal lysozyme crystals. Experiments described reveal that the morphologies of the dissolving crystals at low and high levels of undersaturations go through wholly different habitus. Rounding and diminishing the crystal happens at low undersaturation. Dissolution at higher undersaturation revealed development of ribbed crystal habitus, never noticed for dissolving low molecular weight crystals. Its formation could be explained with specific distribution of energetic places on the crystal surface. Existence of such energetic places is conditioned by inner channels passing through the crystal. A model relating these channels distribution and shapes observed during dissolving is presented.
Publisher
Research Square Platform LLC
Reference34 articles.
1. Giege R, Ducruix A (eds) (1999) Crystallization of Nucleic Acids and Proteins : A Practical Approach. Oxford University Press Inc., New York, pp 278–312
2. ) Nucleation;Vekilov PG;Cryst Growth Des,2010
3. Protein crystallization: From purified protein to diffraction-quality crystal;Chayen NE;Nat Methods,2008
4. Two-Step Mechanism of Macromolecular Nucleation and Crystallization: Field Theory and Simulations;L’vov PE;Cryst Growth Des,2020
5. A review on recent advances for nucleants and nucleation in protein crystallization;Zhou RB;CrystEngComm,2017