Acoustic Focusing of Lysozyme Crystals

Sammanfattning: Acoustic focusing of microscale protein crystals with acoustophoresis technology could reduce clogs during experiments with the scientific technique serial femtosecond x-ray crystallography (SFX). SFX determines molecular structures of proteins, these structures are valuable in drug discovery and fundamental biomedical research. Lysozyme crystals were focused in their own mother liquor and dilutions with PBS buffer. The aim of these tests were to study how the acoustic contrast factor Φ changes with the medium. Recorded experiments were analyzed using the particle tracking software Trackmate to extract velocities and radii. The lysozyme crystals changed morphologies in large dilutions of PBS buffert, they either became rounder or broke into fragments. The changed forms are likely caused by dissolution behaviors; some dilutions were unstable, but not unstable enough to dissolve the crystals completely.  Measured velocities during focusing of the crystals had large variance. Sinusoidal fits of the velocities had significant increases in amplitudes for larger dilutions of PBS. A change in acoustic contrast factor Φ could be the cause for the increased amplitudes, but the results do not rule out other causes. There are currently major knowledge gaps about using protein crystals as particles with acoustophoresis technologies, hence many ideas for future works have been proposed in this master thesis report.