Crystallization of Azotobacter vinelandii Nitrogenase Iron Protein
The iron protein from Azotobacter vinelandii nitrogenase has been crystallized in the reduced form. The needle-shaped crystals are in space group P2_12_12 (a = 94.6 Å, b = 179.9 Å, c = 74.1 Å) and diffract to at least 3.5-Å resolution. Five or six Fe-protein monomers are present in the asymmetric unit.
Additional Information© 1984 American Society for Biochemistry and Molecular Biology. Received for publication, June 7, 1983. This work was supported by Grant 5901-0410-80106 from the Science and Education Administration of the United States Department of Agriculture. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. Partially supported by the Dreyfus Foundation and the donors of the Petroleum Research Foundation, administered by the American Chemical Society. We would like to acknowledge the hospitality of Col. W. N. Lipscomb for providing the initial x-ray diffraction facilities.
Published - 19_rees_1984.pdf