Protein crystals orientation in a magnetic field.
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.
Centre de Recherche sur les Mécanismes de la Croissance Cristalline, CRMC2 - CNRS, Campus de Luminy, case 913, F-13288 Marseille CEDEX 09, France.
J P
JP
Astier
S
S
Veesler
R
R
Boistelle
D000818:Animals; D007611:Aprotinin / Q000737:chemistry / Q000302:isolation & purification; D002417:Cattle; D002645:Chickens; D003460:Crystallization; D004574:Electromagnetic Fields; D009113:Muramidase / Q000737:chemistry / Q000302:isolation & purification; D011506:Proteins / Q000737:chemistry*; D013552:Swine; D000516:alpha-Amylases / Q000737:chemistry / Q000302:isolation & purification
D011506:Proteins; D007611:Aprotinin; D000516:alpha-Amylases; D009113:Muramidase