Scientists in a workshop on Monday expect to make a significant step in understanding the chemical structure of nitrogenase, the key protein that converts nitrogen from the air into a biologically useful form at room temperature and atmospheric pressures. Although nitrogen is important to all forms of life, only a few species of microorganisms can fix atmospheric nitrogen into ammonia and compounds necessary for life. By simulating this natural nitrogenase system, researchers hope to develop eventually a simpler, cheaper way of providing ammonia salts for fertilizer, especially important for agriculture in developing countries. The first step in understanding how nitrogenase works is determining its structure. Results from two different techniques for observing nitrogenase may yield the clearest structure so far. One technique, X-ray diffraction, has given a fuzzy view of the whole protein, roughly showing hundreds of amino acids wrapped around 30 iron atoms and two molybdenum atoms. "People generally understand that the reaction occurs around the metal clusters," says Stephen P. Cramer, a professor of applied science at UC Davis who studies nitrogenase using X-ray absorption. Findings by Cramer, UC Davis colleagues and other collaborators have sharpened the focus on the arrangement of metal atoms within the nitrogenase. By the end of the workshop, the researchers hope to have worked out the basic details of the structure, which resembles a cubist wedding cake. Cramer will present his findings Monday, Aug. 24, 11:05 a.m., Ramada Techworld, South Salon, Grand Ballroom Level. Also, postdoctoral researcher Jie Chen and graduate student Jason Christiansen will present posters on certain details of their work.