An investigation of magnetic field effects on the dissolution of lysozyme crystal and related phenomena

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 58; no. 12; pp. 2024 - 2030
• Main Authors: Yin, D. C., Inatomi, Y., Wakayama, N. I., Huang, W. D., Kuribayashi, K.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England Munksgaard International Publishers 01.12.2002
• Subjects: Crystallization; lysozyme; magnetic field effects; Magnetics; Muramidase - chemistry; protein dissolution
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444902015524

It is now widely known that a magnetic field, either homogeneous or inhomogeneous, depresses the growth process of protein crystals. In this report, the dissolution process of tetragonal lysozyme crystals is also confirmed to be depressed by a homogeneous magnetic field (inhomogeneity <1.5%). The dissolution process was monitored using a Mach–Zehnder interferometer. The results showed that the concentration change during the dissolution process was slowed in a magnetic field compared with that in the absence of a magnetic field. It was concluded that the diffusion coefficient of the lysozyme molecules in the solution was decreased by the magnetic field. The decrease in the diffusion coefficient may contribute to the slowed growth process. The changes in the spatial concentration distribution under a vertical temperature gradient before crystallization in the absence of a magnetic field was also studied. The concentration in the lower, colder part of the cell increased, while it decreased in the upper, hotter part, a similar phenomenon to that discovered by previous investigators in an isothermal supersaturated solution system. Aggregated domain formation is proposed to explain the concentration redistribution before crystal growth and a suspended crystal model is proposed to explain the decrease of diffusivity in a magnetic field.