Thirty years ago the determination of a protein structure required years of effort and typically was sufficient for a Ph.D. thesis. Today, due to advances in synchrotron X-ray sources and detectors, protein crystal structures can be calculated in just hours, "enabling many types of studies that were previously inconceivable," according to a leading researcher at Cornell University, Ithaca, N.Y.
Sol Gruner, a Cornell physics professor and an expert in designing and building fast, large-area X-ray imaging detectors, says that high-powered synchrotron X-ray sources and advanced detectors have been largely responsible for the progress in calculating protein structures. "The biotechnological revolution of the last two decades is built upon the twin pillars of protein structure determination and genetic engineering," he says.
Indeed, says Gruner, "Synchrotron X-radiation has become an enormously powerful tool throughout science and technology."
David Brand | Cornell News
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