Interview of Rees Bryant: Updates from Nigeria

Huffard interviews Bryant on his experiences in the mission field in . The interview was conducted in Searcy, AR

Interview of Rees Bryant

Wright interviews Bryant on his experiences in the mission field in Nigeria. The interview was conducted in Searcy, AR

Newsletter No. I

Newsletter No. I written by Rees Odeil Bryant dated 1 March 1958. Bryant updates his readers on the final preparations for their travels to Nigeria

\u3ci\u3eNewsletter No. 4\u3c/i\u3e

Newsletter No. 4 dated 1 May 1958 written by Patti Mattox Bryant from Nigeria. In the newsletter she describes their adjustments to Nigeria and their ongoing ministry

Finding aid for Rees Odeil and Patti Mattox Bryant Papers

Finding aid for the Rees Odeil and Patti Mattox Bryant Papers

Rees Odeil and Patti Mattox Bryant Papers, (1957-2007)

Finding aid for the Rees Odeil and Patti Mattox Bryant Papers, (1957-2007)

\u3ci\u3eNewsletter No. 3\u3c/i\u3e

Newsletter No. 3 from Rees and Patti Bryant dated 1 May 1958. In the newsletter the Bryants write about the ministry opportunities they had during the month of April

Cross-linking of Nitrogenase Components: Structure and Activity of the Covalent Complex

The nitrogenase complex from Azotobacter vinelandii is composed of the MoFe protein (Av1), an α_2β_2 tetramer, and the Fe protein (Av2), a γ_2 dimer. During turnover of the enzyme, electrons are transferred from Av2 to Av1 in parallel with the hydrolysis of MgATP. Using the cross-linking reagent, 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide, we have identified some of the properties of the complex between the two components. The cross-linking reaction was highly specific yielding a single apparent M_r = 97,000 protein. The amount of cross-linked product was essentially independent of whether MgATP or MgADP were in the reaction. Also, the amount was maximum at high ratios of Av2 to Av1. The M_r = 97,000 protein was characterized by amino acid analysis and Edman degradation and was found to be consistent with a 1:1 complex of an Av2 γ subunit and an Av1 β subunit (the amino terminal serine subunit). The complex was no longer active in the nitrogenase reaction which supports, but does not prove, the requirement for dissociation of the complex after each electron transferred. Nitrogenase activity and cross-linking were inhibited in an identical way by NaCl, which suggests that electrostatic forces are critical to the formation of the electron transfer complex

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