Abstract
A new strategy is proposed for batch crystallization of proteins in solution-growth or gel-growth by using the batch method inside capillary tubes applying magnetic fields. Four proteins with differing proportions of α-helices and β-sheets and crystallized in five different crystallographic space groups are studied, allowing an analysis of the anisotropy of the diamagnetic susceptibility of the peptide bond as well as the polarity of the space groups in the presence of a strong magnetic field of 11.75 T. The crystal quality is shown to be improved by using a strong magnetic field to orient protein molecules, and gel-growth (high concentrations of agar) to control the transport phenomena as well as crystal growth. Some advantages to increase the crystal quality for crystals from marginal conditions for X-ray diffraction, and disadvantages of the use of solution- and gel-growth (low concentration of agar) in magnetic fields, and their plausible applications to high resolution X-ray crystallography are discussed.
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