Abstract
High-quality crystals are essential to ensure high-resolution structural information. Protein crystals are controlled by many factors, such as pH, temperature, and the ion concentration of crystalline solutions. We previously reported the development of a device dedicated to protein crystallization. In the current study, we have further modified and improved our device. Exposure to external magnetic field leads to alignment of the crystal toward a preferred direction depending on the magnetization energy. Each material has different magnetic susceptibilities depending on the individual direction of their unit crystal cells. One of the strategies to acquire a large crystal entails controlling the nucleation rate. Furthermore, exposure of a crystal to a magnetic field may lead to new morphologies by affecting the crystal volume, shape, and quality.
Highlights
Many biological systems are composed of neighboring atoms bonded by various hydrogen atoms [1,2]
Depending onmagnetic the magnetic fieldapplied, applied, aa difference was observed during the lysozyme
Depending on the field difference was observed during the lysozyme crystallization process (Figure 4)
Summary
Many biological systems are composed of neighboring atoms bonded by various hydrogen atoms [1,2]. It is believed that hydrogen atoms play a crucial role in biological functions, such as enzymatic mechanisms [3,4]. The precise localization of the hydrogen atoms in biological problems is more important than in other systems, for example, in the case of solid-state physics [1,5,6]. It has limitations due to the interactions of the X-rays with electrons of the atoms in the crystal structure. It is impossible to localize the relative position of the light atoms, such as H or Li, in the presence of a relative heavy atom in a crystal structure. Several sophisticated tools have been developed to delineate the location of the hydrogen atoms and, if possible, to distinguish isotopes such as hydrogen and deuterium [9,10]
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