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Neutron small angle scattering of the Mo-Fe protein (nitrogenase) from Clostridium pasteurianum
Authors:Jacques Meyer  Giuseppe Zaccai
Institution:1. Laboratoire de Biochimie (CNRS/ER 235 et INSERM U. 191) Département de Recherche Fondamentale, Centre d''Etudes Nucléaires, 85X, 38041 Grenoble cedex, France;2. Institut Laüe-Langevin, 156X, 38042 Grenoble cedex, France
Abstract:Neutron small angle scattering measurements of solutions of the Mo-Fe protein from C. pasteurianum have yielded the following results. The molecular weight of the protein is 208,000 ± 10,000, in agreement with figures obtained by other methods. The radius of gyration is 39.8 ± 0.7 Å in H2O, and 37.6 ± 0.3 Å in D2O. The experimental scattering curves have been compared with the calculated scattering curves of simple homogeneous bodies. It is concluded that the MoFe protein from C. pasteurianum is a non spherical particle having an axial ratio of 2:1, and that it probably has little, if any, solvent containing cavities.
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