A new strategy is proposed for protein crystallization methods in solution-growth or gel-growth by using different crystal growth devices applying electric (in the range of micro-Amperes) and magnetic fields (from 7 to 12 Tesla). The effect of combining both electric and magnetic fields is shown and is reviewed. Proteins with differing contents of a-helices and b-sheets, and crystallized in different crystallographic space groups are studied. The crystal quality is improved by using an electric field to electro-migrate ions to the ITO electrodes, and to orientate protein molecules by using a strong magnetic field in either solution or gel-growth to control the transport phenomena. Some advantages to increase the crystal quality for crystals from marginal conditions for X-ray diffraction are discussed. Finally, in order to separate the nucleation and the crystal growth processes (by using these electromagnetic fields), the obtainment of either large amount of small crystals for Powder X-ray Diffraction or big single crystals for the classic X-ray Crystallography (or Neutron Diffraction Crystallography) is also evaluated. Acknowledgements: The author (A.M.) gratefully acknowledges financial support from CONACYT-Mexico Project No. 175924.
Universidad Nacional Autonoma de Mexico (UNAM)
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