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Protein crystals orientation in a magnetic field
J P Astier1, S Veesler, R Boistelle
1Centre de Recherche sur les Mécanismes de la Croissance Cristalline, CRMC2 - CNRS, Campus de Luminy, case 913, F-13288 Marseille CEDEX 09, France.
Abstract:
Nucleation and crystal growth of hen egg-white lysozyme, bovine pancreatic trypsin inhibitor and porcine pancreatic alpha-amylase were carried out in the presence of a magnetic field of 1.25 T produced by small permanent magnets. Crystals were oriented in the magnetic field, except when heterogeneous nucleation occurred. The orientation of protein crystals in the presence of a magnetic field can be attributed to the anisotropic diamagnetic susceptibility of proteins resulting from the large anisotropy of the alpha-helices due to the axial alignment of the peptide bonds.